FREE SHIPPING over $40
OVER 10000 FIVE-STAR REVIEWS
5% OFF ALL SUBSCRIPTIONS
100% HAPPINESS GUARANTEE
Analyze Diet
0
Science (New York, N.Y.)1992; 258(5089); 1748-1755; doi: 10.1126/science.1334573

Crystal structure of a complex between electron transfer partners, cytochrome c peroxidase and cytochrome c.

Abstract: The crystal structure of a 1:1 complex between yeast cytochrome c peroxidase and yeast iso-1-cytochrome c was determined at 2.3 A resolution. This structure reveals a possible electron transfer pathway unlike any previously proposed for this extensively studied redox pair. The shortest straight line between the two hemes closely follows the peroxidase backbone chain of residues Ala194, Ala193, Gly192, and finally Trp191, the indole ring of which is perpendicular to, and in van der Waals contact with, the peroxidase heme. The crystal structure at 2.8 A of a complex between yeast cytochrome c peroxidase and horse heart cytochrome c was also determined. Although crystals of the two complexes (one with cytochrome c from yeast and the other with cytochrome c from horse) grew under very different conditions and belong to different space groups, the two complex structures are closely similar, suggesting that cytochrome c interacts with its redox partners in a highly specific manner.
Get Full Text
Publication Date: 1992-12-11 PubMed ID: 1334573DOI: 10.1126/science.1334573Google Scholar: Lookup
The Equine Research Bank provides access to a large database of publicly available scientific literature. Inclusion in the Research Bank does not imply endorsement of study methods or findings by Mad Barn.
LinkedInCopy
  • Journal Article
  • Research Support
  • Non-U.S. Gov't
  • Research Support
  • U.S. Gov't
  • Non-P.H.S.
  • Research Support
  • U.S. Gov't
  • P.H.S.

Summary

This research summary has been generated with artificial intelligence and may contain errors and omissions. Refer to the original study to confirm details provided. Submit correction.

The research focuses on the understanding of the electron transfer mechanism in yeast, specifically between cytochrome c peroxidase and cytochrome c, by means of analyzing their crystal structures at a 2.3 A resolution. The paper reveals an unprecedented pathway for this transfer, terminating at Trp191. Similar observations were also conducted for the horse heart cytochrome c.

Overview of the Research

  • The researchers present an in-depth analysis of the crystal structure of a 1:1 complex between yeast cytochrome c peroxidase and yeast iso-1-cytochrome c. The crystal structure was determined at a resolution of 2.3 A.
  • From this analysis, they identify a possible route for electron transfer. This route is unlike any proposed previously for this redox pair, which has been extensively studied.

Electron Transfer Pathway

  • In this newly discovered electron transfer pathway, the shortest straight line between the two hemes closely follows the peroxidase backbone chain of residues Ala194, Ala193, Gly192, and finally Trp191.
  • Trp191’s indole ring is positioned perpendicular to and in van der Waals contact with the peroxidase heme, indicating the site of electron transfer.

Comparative Study with Horse Heart Cytochrome c

  • The researchers also examined the crystal structure of a complex between yeast cytochrome c peroxidase and horse heart cytochrome c at a resolution of 2.8 A.
  • Although the conditions under which the crystals for these two complexes (one with cytochrome c from yeast, the other with cytochrome c from a horse) were grown differed substantially and belonged to differing space groups, the structures of the two complexes were found to be very similar.
  • This suggests that cytochrome c interacts with its redox partners in a highly specific manner, irrespective of the source of cytochrome c.

Conclusion

  • In summary, the research provides new insights into the mechanism of electron transfer between cytochrome c peroxidase and cytochrome c, a significant process in energy production. The findings indicate a unique pathway for electron transfer and highlight the specificity of interaction between cytochrome c and its redox partners.

Cite This Article

APA
Pelletier H, Kraut J. (1992). Crystal structure of a complex between electron transfer partners, cytochrome c peroxidase and cytochrome c. Science, 258(5089), 1748-1755. https://doi.org/10.1126/science.1334573

Publication

Science (New York, N.Y.)
ISSN: 0036-8075
NlmUniqueID: 0404511
Country: United States
Language: English
Volume: 258
Issue: 5089
Pages: 1748-1755

Researcher Affiliations

Pelletier, H
  • Department of Chemistry, University of California, San Diego, La Jolla 92093-0317.
Kraut, J

    MeSH Terms

    • Amino Acid Sequence
    • Animals
    • Binding Sites
    • Cytochrome c Group / chemistry
    • Cytochrome c Group / metabolism
    • Cytochrome-c Peroxidase / chemistry
    • Cytochrome-c Peroxidase / metabolism
    • Electron Transport
    • Heme / metabolism
    • Horses
    • Models, Molecular
    • Molecular Sequence Data
    • Protein Conformation
    • Saccharomyces cerevisiae / metabolism
    • X-Ray Diffraction / methods

    Grant Funding

    • DK07233 / NIDDK NIH HHS

    Citations

    This article has been cited 140 times.
    1. Fang W, Feng S, Jiang Z, Liang W, Li P, Wang B. Understanding the Key Roles of pH Buffer in Accelerating Lignin Degradation by Lignin Peroxidase. JACS Au 2023 Feb 27;3(2):536-549.
      doi: 10.1021/jacsau.2c00649pubmed: 36873691google scholar: lookup
    2. Brand SE, Scharlau M, Geren L, Hendrix M, Parson C, Elmendorf T, Neel E, Pianalto K, Silva-Nash J, Durham B, Millett F. Accelerated Evolution of Cytochrome c in Higher Primates, and Regulation of the Reaction between Cytochrome c and Cytochrome Oxidase by Phosphorylation. Cells 2022 Dec 12;11(24).
      doi: 10.3390/cells11244014pubmed: 36552779google scholar: lookup
    3. Oohora K, Tomoda H, Hayashi T. Reactivity of Myoglobin Reconstituted with Cobalt Corrole toward Hydrogen Peroxide. Int J Mol Sci 2022 Apr 27;23(9).
      doi: 10.3390/ijms23094829pubmed: 35563217google scholar: lookup
    4. Khoroshyy P, Tenger K, Chertkova RV, Bocharova OV, Kirpichnikov MP, Borovok N, Groma GI, Dolgikh DA, Kotlyar AB, Zimányi L. Kinetics and Energetics of Intramolecular Electron Transfer in Single-Point Labeled TUPS-Cytochrome c Derivatives. Molecules 2021 Nov 18;26(22).
      doi: 10.3390/molecules26226976pubmed: 34834068google scholar: lookup
    5. Gamero-Quijano A, Bhattacharya S, Cazade PA, Molina-Osorio AF, Beecher C, Djeghader A, Soulimane T, Dossot M, Thompson D, Herzog G, Scanlon MD. Modulating the pro-apoptotic activity of cytochrome c at a biomimetic electrified interface. Sci Adv 2021 Nov 5;7(45):eabg4119.
      doi: 10.1126/sciadv.abg4119pubmed: 34739310google scholar: lookup
    6. Vilbert AC, Liu Y, Dai H, Lu Y. Recent advances in tuning redox properties of electron transfer centers in metalloenzymes catalyzing oxygen reduction reaction and H(2) oxidation important for fuel cells design. Curr Opin Electrochem 2021 Dec;30.
      doi: 10.1016/j.coelec.2021.100780pubmed: 34435160google scholar: lookup
    7. Di Savino A, Foerster JM, Ullmann GM, Ubbink M. Enhancing the population of the encounter complex affects protein complex formation efficiency. FEBS J 2022 Jan;289(2):535-548.
      doi: 10.1111/febs.16159pubmed: 34403572google scholar: lookup
    8. Kölsch A, Radon C, Golub M, Baumert A, Bürger J, Mielke T, Lisdat F, Feoktystov A, Pieper J, Zouni A, Wendler P. Current limits of structural biology: The transient interaction between cytochrome c (6) and photosystem I. Curr Res Struct Biol 2020;2:171-179.
      doi: 10.1016/j.crstbi.2020.08.003pubmed: 34235477google scholar: lookup
    9. Liu S, Xu J, Li X, Yan T, Yu S, Sun H, Liu J. Template-Free Self-Assembly of Two-Dimensional Polymers into Nano/Microstructured Materials. Molecules 2021 May 31;26(11).
      doi: 10.3390/molecules26113310pubmed: 34072932google scholar: lookup
    10. Kwon H, Basran J, Pathak C, Hussain M, Freeman SL, Fielding AJ, Bailey AJ, Stefanou N, Sparkes HA, Tosha T, Yamashita K, Hirata K, Murakami H, Ueno G, Ago H, Tono K, Yamamoto M, Sawai H, Shiro Y, Sugimoto H, Raven EL, Moody PCE. XFEL Crystal Structures of Peroxidase Compound II. Angew Chem Int Ed Engl 2021 Jun 21;60(26):14578-14585.
      doi: 10.1002/anie.202103010pubmed: 33826799google scholar: lookup
    11. Di Savino A, Foerster JM, Ullmann GM, Ubbink M. The Charge Distribution on a Protein Surface Determines Whether Productive or Futile Encounter Complexes Are Formed. Biochemistry 2021 Mar 16;60(10):747-755.
      doi: 10.1021/acs.biochem.1c00021pubmed: 33646750google scholar: lookup
    12. Kawakami T, Yu LJ, Liang T, Okazaki K, Madigan MT, Kimura Y, Wang-Otomo ZY. Crystal structure of a photosynthetic LH1-RC in complex with its electron donor HiPIP. Nat Commun 2021 Feb 17;12(1):1104.
      doi: 10.1038/s41467-021-21397-9pubmed: 33597527google scholar: lookup
    13. Giampà M, Sgobba E. Insight to Functional Conformation and Noncovalent Interactions of Protein-Protein Assembly Using MALDI Mass Spectrometry. Molecules 2020 Oct 28;25(21).
      doi: 10.3390/molecules25214979pubmed: 33126406google scholar: lookup
    14. Di Savino A, Foerster JM, La Haye T, Blok A, Timmer M, Ullmann GM, Ubbink M. Efficient Encounter Complex Formation and Electron Transfer to Cytochrome c Peroxidase with an Additional, Distant Electrostatic Binding Site. Angew Chem Int Ed Engl 2020 Dec 14;59(51):23239-23243.
      doi: 10.1002/anie.202010006pubmed: 32827196google scholar: lookup
    15. van Son M, Schilder JT, Di Savino A, Blok A, Ubbink M, Huber M. The Transient Complex of Cytochrome c and Cytochrome c Peroxidase: Insights into the Encounter Complex from Multifrequency EPR and NMR Spectroscopy. Chemphyschem 2020 May 18;21(10):1060-1069.
      doi: 10.1002/cphc.201901160pubmed: 32301564google scholar: lookup
    16. Yee EF, Dzikovski B, Crane BR. Tuning Radical Relay Residues by Proton Management Rescues Protein Electron Hopping. J Am Chem Soc 2019 Nov 6;141(44):17571-17587.
      doi: 10.1021/jacs.9b05715pubmed: 31603693google scholar: lookup
    17. Foerster JM, Poehner I, Ullmann GM. MCMap-A Computational Tool for Mapping Energy Landscapes of Transient Protein-Protein Interactions. ACS Omega 2018 Jun 30;3(6):6465-6475.
      doi: 10.1021/acsomega.8b00572pubmed: 31458826google scholar: lookup
    18. Hallen MA, Martin JW, Ojewole A, Jou JD, Lowegard AU, Frenkel MS, Gainza P, Nisonoff HM, Mukund A, Wang S, Holt GT, Zhou D, Dowd E, Donald BR. OSPREY 3.0: Open-source protein redesign for you, with powerful new features. J Comput Chem 2018 Nov 15;39(30):2494-2507.
      doi: 10.1002/jcc.25522pubmed: 30368845google scholar: lookup
    19. Wang J, Liu Z, Crabtree RH, Frank J, Moore PB. On the damage done to the structure of the Thermoplasma acidophilum proteasome by electron radiation. Protein Sci 2018 Dec;27(12):2051-2061.
      doi: 10.1002/pro.3511pubmed: 30242932google scholar: lookup
    20. Deng Y, Zhong F, Alden SL, Hoke KR, Pletneva EV. The K79G Mutation Reshapes the Heme Crevice and Alters Redox Properties of Cytochrome c. Biochemistry 2018 Oct 9;57(40):5827-5840.
      doi: 10.1021/acs.biochem.8b00650pubmed: 30142276google scholar: lookup
    21. Kölsch A, Hejazi M, Stieger KR, Feifel SC, Kern JF, Müh F, Lisdat F, Lokstein H, Zouni A. Insights into the binding behavior of native and non-native cytochromes to photosystem I from Thermosynechococcus elongatus. J Biol Chem 2018 Jun 8;293(23):9090-9100.
      doi: 10.1074/jbc.RA117.000953pubmed: 29695502google scholar: lookup
    22. Hollingsworth SA, Nguyen BD, Chreifi G, Arce AP, Poulos TL. Insights into the Dynamics and Dissociation Mechanism of a Protein Redox Complex Using Molecular Dynamics. J Chem Inf Model 2017 Sep 25;57(9):2344-2350.
      doi: 10.1021/acs.jcim.7b00421pubmed: 28841378google scholar: lookup
    23. Wang J. On contribution of known atomic partial charges of protein backbone in electrostatic potential density maps. Protein Sci 2017 Jun;26(6):1098-1104.
      doi: 10.1002/pro.3169pubmed: 28370507google scholar: lookup
    24. Shimada S, Shinzawa-Itoh K, Baba J, Aoe S, Shimada A, Yamashita E, Kang J, Tateno M, Yoshikawa S, Tsukihara T. Complex structure of cytochrome c-cytochrome c oxidase reveals a novel protein-protein interaction mode. EMBO J 2017 Feb 1;36(3):291-300.
      doi: 10.15252/embj.201695021pubmed: 27979921google scholar: lookup
    25. Celis AI, Gauss GH, Streit BR, Shisler K, Moraski GC, Rodgers KR, Lukat-Rodgers GS, Peters JW, DuBois JL. Structure-Based Mechanism for Oxidative Decarboxylation Reactions Mediated by Amino Acids and Heme Propionates in Coproheme Decarboxylase (HemQ). J Am Chem Soc 2017 Feb 8;139(5):1900-1911.
      doi: 10.1021/jacs.6b11324pubmed: 27936663google scholar: lookup
    26. Ross MO, Rosenzweig AC. A tale of two methane monooxygenases. J Biol Inorg Chem 2017 Apr;22(2-3):307-319.
      doi: 10.1007/s00775-016-1419-ypubmed: 27878395google scholar: lookup
    27. Hewitt SH, Filby MH, Hayes E, Kuhn LT, Kalverda AP, Webb ME, Wilson AJ. Protein Surface Mimetics: Understanding How Ruthenium Tris(Bipyridines) Interact with Proteins. Chembiochem 2017 Jan 17;18(2):223-231.
      doi: 10.1002/cbic.201600552pubmed: 27860106google scholar: lookup
    28. Singharoy A, Barragan AM, Thangapandian S, Tajkhorshid E, Schulten K. Binding Site Recognition and Docking Dynamics of a Single Electron Transport Protein: Cytochrome c2. J Am Chem Soc 2016 Sep 21;138(37):12077-89.
      doi: 10.1021/jacs.6b01193pubmed: 27508459google scholar: lookup
    29. Payne TM, Yee EF, Dzikovski B, Crane BR. Constraints on the Radical Cation Center of Cytochrome c Peroxidase for Electron Transfer from Cytochrome c. Biochemistry 2016 Aug 30;55(34):4807-22.
      doi: 10.1021/acs.biochem.6b00262pubmed: 27499202google scholar: lookup
    30. Melo R, Fieldhouse R, Melo A, Correia JD, Cordeiro MN, Gümüş ZH, Costa J, Bonvin AM, Moreira IS. A Machine Learning Approach for Hot-Spot Detection at Protein-Protein Interfaces. Int J Mol Sci 2016 Jul 27;17(8).
      doi: 10.3390/ijms17081215pubmed: 27472327google scholar: lookup
    31. Seal M, Ghosh C, Basu O, Dey SG. Cytochrome c peroxidase activity of heme bound amyloid β peptides. J Biol Inorg Chem 2016 Sep;21(5-6):683-90.
      doi: 10.1007/s00775-016-1367-6pubmed: 27270708google scholar: lookup
    32. Schilder J, Ubbink M. Weak self-association of cytochrome c peroxidase molecules observed by paramagnetic NMR. J Biomol NMR 2016 May;65(1):29-40.
      doi: 10.1007/s10858-016-0035-zpubmed: 27236778google scholar: lookup
    33. Dourado DF, Flores SC. Modeling and fitting protein-protein complexes to predict change of binding energy. Sci Rep 2016 May 13;6:25406.
      doi: 10.1038/srep25406pubmed: 27173910google scholar: lookup
    34. Chreifi G, Baxter EL, Doukov T, Cohen AE, McPhillips SE, Song J, Meharenna YT, Soltis SM, Poulos TL. Crystal structure of the pristine peroxidase ferryl center and its relevance to proton-coupled electron transfer. Proc Natl Acad Sci U S A 2016 Feb 2;113(5):1226-31.
      doi: 10.1073/pnas.1521664113pubmed: 26787871google scholar: lookup
    35. McGrath AP, Laming EL, Casas Garcia GP, Kvansakul M, Guss JM, Trewhella J, Calmes B, Bernhardt PV, Hanson GR, Kappler U, Maher MJ. Structural basis of interprotein electron transfer in bacterial sulfite oxidation. Elife 2015 Dec 19;4:e09066.
      doi: 10.7554/eLife.09066pubmed: 26687009google scholar: lookup
    36. Fry BA, Solomon LA, Leslie Dutton P, Moser CC. Design and engineering of a man-made diffusive electron-transport protein. Biochim Biophys Acta 2016 May;1857(5):513-521.
      doi: 10.1016/j.bbabio.2015.09.008pubmed: 26423266google scholar: lookup
    37. Shalaeva DN, Dibrova DV, Galperin MY, Mulkidjanian AY. Modeling of interaction between cytochrome c and the WD domains of Apaf-1: bifurcated salt bridges underlying apoptosome assembly. Biol Direct 2015 May 27;10:29.
      doi: 10.1186/s13062-015-0059-4pubmed: 26014357google scholar: lookup
    38. Van de Water K, Sterckx YG, Volkov AN. The low-affinity complex of cytochrome c and its peroxidase. Nat Commun 2015 May 6;6:7073.
      doi: 10.1038/ncomms8073pubmed: 25944250google scholar: lookup
    39. Chreifi G, Hollingsworth SA, Li H, Tripathi S, Arce AP, Magaña-Garcia HI, Poulos TL. Enzymatic Mechanism of Leishmania major Peroxidase and the Critical Role of Specific Ionic Interactions. Biochemistry 2015 Jun 2;54(21):3328-36.
      doi: 10.1021/acs.biochem.5b00338pubmed: 25941976google scholar: lookup
    40. Page TR, Hoffman BM. Control of cyclic photoinitiated electron transfer between cytochrome c peroxidase (W191F) and cytochrome c by formation of dynamic binary and ternary complexes. Biochemistry 2015 Feb 10;54(5):1188-97.
      doi: 10.1021/bi500888ypubmed: 25629200google scholar: lookup
    41. Sun Y, Benabbas A, Zeng W, Kleingardner JG, Bren KL, Champion PM. Investigations of heme distortion, low-frequency vibrational excitations, and electron transfer in cytochrome c. Proc Natl Acad Sci U S A 2014 May 6;111(18):6570-5.
      doi: 10.1073/pnas.1322274111pubmed: 24753591google scholar: lookup
    42. Richardson JS, Richardson DC. Biophysical highlights from 54 years of macromolecular crystallography. Biophys J 2014 Feb 4;106(3):510-25.
      doi: 10.1016/j.bpj.2014.01.001pubmed: 24507592google scholar: lookup
    43. Poulos TL. Heme enzyme structure and function. Chem Rev 2014 Apr 9;114(7):3919-62.
      doi: 10.1021/cr400415kpubmed: 24400737google scholar: lookup
    44. Gan L, Liu Z, Zhang Z, Yang X, Liu J, Sun C. SOCS2 inhibited mitochondria biogenesis via inhibiting p38 MAPK/ATF2 pathway in C2C12 cells. Mol Biol Rep 2014 Feb;41(2):627-37.
      doi: 10.1007/s11033-013-2901-zpubmed: 24352701google scholar: lookup
    45. Jiang N, Kuznetsov A, Nocek JM, Hoffman BM, Crane BR, Hu X, Beratan DN. Distance-independent charge recombination kinetics in cytochrome c-cytochrome c peroxidase complexes: compensating changes in the electronic coupling and reorganization energies. J Phys Chem B 2013 Aug 8;117(31):9129-41.
      doi: 10.1021/jp401551tpubmed: 23895339google scholar: lookup
    46. Volkov AN, van Nuland NA. Solution NMR study of the yeast cytochrome c peroxidase: cytochrome c interaction. J Biomol NMR 2013 Jul;56(3):255-63.
      doi: 10.1007/s10858-013-9744-8pubmed: 23708935google scholar: lookup
    47. Zaidi S, Hassan MI, Islam A, Ahmad F. The role of key residues in structure, function, and stability of cytochrome-c. Cell Mol Life Sci 2014 Jan;71(2):229-55.
      doi: 10.1007/s00018-013-1341-1pubmed: 23615770google scholar: lookup
    48. Kawai C, Pessoto FS, Graves CV, Carmona-Ribeiro AM, Nantes IL. Effects of transmembrane potential and pH gradient on the cytochrome c-promoted fusion of mitochondrial mimetic membranes. J Bioenerg Biomembr 2013 Aug;45(4):421-30.
      doi: 10.1007/s10863-013-9507-ypubmed: 23564075google scholar: lookup
    49. Wallrapp FH, Voityuk AA, Guallar V. In-silico assessment of protein-protein electron transfer. a case study: cytochrome c peroxidase--cytochrome c. PLoS Comput Biol 2013;9(3):e1002990.
      doi: 10.1371/journal.pcbi.1002990pubmed: 23555224google scholar: lookup
    50. Kang JH. Salsolinol, a catechol neurotoxin, induces oxidative modification of cytochrome c. BMB Rep 2013 Feb;46(2):119-23.
      doi: 10.5483/bmbrep.2013.46.2.220pubmed: 23433116google scholar: lookup
    51. Volkov AN, van Nuland NA. Electron transfer interactome of cytochrome C. PLoS Comput Biol 2012;8(12):e1002807.
      doi: 10.1371/journal.pcbi.1002807pubmed: 23236271google scholar: lookup
    52. Jasion VS, Doukov T, Pineda SH, Li H, Poulos TL. Crystal structure of the Leishmania major peroxidase-cytochrome c complex. Proc Natl Acad Sci U S A 2012 Nov 6;109(45):18390-4.
      doi: 10.1073/pnas.1213295109pubmed: 23100535google scholar: lookup
    53. Ravikumar KM, Huang W, Yang S. Coarse-grained simulations of protein-protein association: an energy landscape perspective. Biophys J 2012 Aug 22;103(4):837-45.
      doi: 10.1016/j.bpj.2012.07.013pubmed: 22947945google scholar: lookup
    54. Galinato MG, Kleingardner JG, Bowman SE, Alp EE, Zhao J, Bren KL, Lehnert N. Heme-protein vibrational couplings in cytochrome c provide a dynamic link that connects the heme-iron and the protein surface. Proc Natl Acad Sci U S A 2012 Jun 5;109(23):8896-900.
      doi: 10.1073/pnas.1200345109pubmed: 22619327google scholar: lookup
    55. Scanu S, Förster J, Finiguerra MG, Shabestari MH, Huber M, Ubbink M. The complex of cytochrome f and plastocyanin from Nostoc sp. PCC 7119 is highly dynamic. Chembiochem 2012 Jun 18;13(9):1312-8.
      doi: 10.1002/cbic.201200073pubmed: 22619165google scholar: lookup
    56. Lin MT, Gennis RB. Product-controlled steady-state kinetics between cytochrome aa(3) from Rhodobacter sphaeroides and equine ferrocytochrome c analyzed by a novel spectrophotometric approach. Biochim Biophys Acta 2012 Oct;1817(10):1894-900.
      doi: 10.1016/j.bbabio.2012.04.001pubmed: 22516686google scholar: lookup
    57. Meng XY, Xu Y, Zhang HX, Mezei M, Cui M. Predicting protein interactions by Brownian dynamics simulations. J Biomed Biotechnol 2012;2012:121034.
      doi: 10.1155/2012/121034pubmed: 22500075google scholar: lookup
    58. Jasion VS, Poulos TL. Leishmania major peroxidase is a cytochrome c peroxidase. Biochemistry 2012 Mar 27;51(12):2453-60.
      doi: 10.1021/bi300169xpubmed: 22372542google scholar: lookup
    59. Yan Y, Zhang S, Wu FX. Applications of graph theory in protein structure identification. Proteome Sci 2011 Oct 14;9 Suppl 1(Suppl 1):S17.
      doi: 10.1186/1477-5956-9-S1-S17pubmed: 22165974google scholar: lookup
    60. Díaz-Moreno I, García-Heredia JM, Díaz-Quintana A, De la Rosa MA. Cytochrome c signalosome in mitochondria. Eur Biophys J 2011 Dec;40(12):1301-15.
      doi: 10.1007/s00249-011-0774-4pubmed: 22086608google scholar: lookup
    61. Sakamoto K, Kamiya M, Imai M, Shinzawa-Itoh K, Uchida T, Kawano K, Yoshikawa S, Ishimori K. NMR basis for interprotein electron transfer gating between cytochrome c and cytochrome c oxidase. Proc Natl Acad Sci U S A 2011 Jul 26;108(30):12271-6.
      doi: 10.1073/pnas.1108320108pubmed: 21746907google scholar: lookup
    62. Dell'acqua S, Moura I, Moura JJ, Pauleta SR. The electron transfer complex between nitrous oxide reductase and its electron donors. J Biol Inorg Chem 2011 Dec;16(8):1241-54.
      doi: 10.1007/s00775-011-0812-9pubmed: 21739254google scholar: lookup
    63. Jasion VS, Polanco JA, Meharenna YT, Li H, Poulos TL. Crystal structure of Leishmania major peroxidase and characterization of the compound i tryptophan radical. J Biol Chem 2011 Jul 15;286(28):24608-15.
      doi: 10.1074/jbc.M111.230524pubmed: 21566139google scholar: lookup
    64. Bertini I, Chevance S, Del Conte R, Lalli D, Turano P. The anti-apoptotic Bcl-x(L) protein, a new piece in the puzzle of cytochrome c interactome. PLoS One 2011 Apr 18;6(4):e18329.
      doi: 10.1371/journal.pone.0018329pubmed: 21533126google scholar: lookup
    65. Lederer F. Another look at the interaction between mitochondrial cytochrome c and flavocytochrome b (2). Eur Biophys J 2011 Dec;40(12):1283-99.
      doi: 10.1007/s00249-011-0697-0pubmed: 21503671google scholar: lookup
    66. Kastritis PL, Moal IH, Hwang H, Weng Z, Bates PA, Bonvin AM, Janin J. A structure-based benchmark for protein-protein binding affinity. Protein Sci 2011 Mar;20(3):482-91.
      doi: 10.1002/pro.580pubmed: 21213247google scholar: lookup
    67. Filby MH, Muldoon J, Dabb S, Fletcher NC, Ashcroft AE, Wilson AJ. Protein surface recognition using geometrically pure Ru(II) tris(bipyridine) derivatives. Chem Commun (Camb) 2011 Jan 7;47(1):559-61.
      doi: 10.1039/c0cc04754fpubmed: 21103575google scholar: lookup
    68. Volkov AN, Ubbink M, van Nuland NA. Mapping the encounter state of a transient protein complex by PRE NMR spectroscopy. J Biomol NMR 2010 Dec;48(4):225-36.
      doi: 10.1007/s10858-010-9452-6pubmed: 21049303google scholar: lookup
    69. Kokhan O, Wraight CA, Tajkhorshid E. The binding interface of cytochrome c and cytochrome c₁ in the bc₁ complex: rationalizing the role of key residues. Biophys J 2010 Oct 20;99(8):2647-56.
      doi: 10.1016/j.bpj.2010.08.042pubmed: 20959106google scholar: lookup
    70. Goblirsch BR, Streit BR, Dubois JL, Wilmot CM. Structural features promoting dioxygen production by Dechloromonas aromatica chlorite dismutase. J Biol Inorg Chem 2010 Aug;15(6):879-88.
      doi: 10.1007/s00775-010-0651-0pubmed: 20386942google scholar: lookup
    71. Poulos TL. Thirty years of heme peroxidase structural biology. Arch Biochem Biophys 2010 Aug 1;500(1):3-12.
      doi: 10.1016/j.abb.2010.02.008pubmed: 20206121google scholar: lookup
    72. Muldoon J, Ashcroft AE, Wilson AJ. Selective protein-surface sensing using ruthenium(II) tris(bipyridine) complexes. Chemistry 2010 Jan 4;16(1):100-3.
      doi: 10.1002/chem.200902368pubmed: 19946912google scholar: lookup
    73. Nojiri M, Koteishi H, Nakagami T, Kobayashi K, Inoue T, Yamaguchi K, Suzuki S. Structural basis of inter-protein electron transfer for nitrite reduction in denitrification. Nature 2009 Nov 5;462(7269):117-20.
      doi: 10.1038/nature08507pubmed: 19890332google scholar: lookup
    74. Smith AT, Doyle WA, Dorlet P, Ivancich A. Spectroscopic evidence for an engineered, catalytically active Trp radical that creates the unique reactivity of lignin peroxidase. Proc Natl Acad Sci U S A 2009 Sep 22;106(38):16084-9.
      doi: 10.1073/pnas.0904535106pubmed: 19805263google scholar: lookup
    75. Clore GM, Iwahara J. Theory, practice, and applications of paramagnetic relaxation enhancement for the characterization of transient low-population states of biological macromolecules and their complexes. Chem Rev 2009 Sep;109(9):4108-39.
      doi: 10.1021/cr900033ppubmed: 19522502google scholar: lookup
    76. Ruiz-Dueñas FJ, Pogni R, Morales M, Giansanti S, Mate MJ, Romero A, Martínez MJ, Basosi R, Martínez AT. Protein radicals in fungal versatile peroxidase: catalytic tryptophan radical in both compound I and compound II and studies on W164Y, W164H, and W164S variants. J Biol Chem 2009 Mar 20;284(12):7986-94.
      doi: 10.1074/jbc.M808069200pubmed: 19158088google scholar: lookup
    77. Hays Putnam AM, Lee YT, Goodin DB. Replacement of an electron transfer pathway in cytochrome c peroxidase with a surrogate peptide. Biochemistry 2009 Jan 13;48(1):1-3.
      doi: 10.1021/bi8020263pubmed: 19072042google scholar: lookup
    78. Janzon J, Yuan Q, Malatesta F, Hellwig P, Ludwig B, Durham B, Millett F. Probing the Paracoccus denitrificans cytochrome c(1)-cytochrome c(552) interaction by mutagenesis and fast kinetics. Biochemistry 2008 Dec 9;47(49):12974-84.
      doi: 10.1021/bi800932cpubmed: 19006325google scholar: lookup
    79. Meharenna YT, Oertel P, Bhaskar B, Poulos TL. Engineering ascorbate peroxidase activity into cytochrome c peroxidase. Biochemistry 2008 Sep 30;47(39):10324-32.
      doi: 10.1021/bi8007565pubmed: 18771292google scholar: lookup
    80. Guallar V, Wallrapp F. Mapping protein electron transfer pathways with QM/MM methods. J R Soc Interface 2008 Dec 6;5 Suppl 3(Suppl 3):S233-9.
      doi: 10.1098/rsif.2008.0061.focuspubmed: 18445553google scholar: lookup
    81. Davidson VL. Protein control of true, gated, and coupled electron transfer reactions. Acc Chem Res 2008 Jun;41(6):730-8.
      doi: 10.1021/ar700252cpubmed: 18442271google scholar: lookup
    82. Michel LV, Bren KL. Submolecular unfolding units of Pseudomonas aeruginosa cytochrome c-551. J Biol Inorg Chem 2008 Jun;13(5):837-45.
      doi: 10.1007/s00775-008-0370-ypubmed: 18392863google scholar: lookup
    83. Meyer B, Kuever J. Homology modeling of dissimilatory APS reductases (AprBA) of sulfur-oxidizing and sulfate-reducing prokaryotes. PLoS One 2008 Jan 30;3(1):e1514.
      doi: 10.1371/journal.pone.0001514pubmed: 18231600google scholar: lookup
    84. Kim YC, Hummer G. Coarse-grained models for simulations of multiprotein complexes: application to ubiquitin binding. J Mol Biol 2008 Feb 1;375(5):1416-33.
      doi: 10.1016/j.jmb.2007.11.063pubmed: 18083189google scholar: lookup
    85. Pearl NM, Jacobson T, Arisa M, Vitello LB, Erman JE. Effect of single-site charge-reversal mutations on the catalytic properties of yeast cytochrome c peroxidase: mutations near the high-affinity cytochrome c binding site. Biochemistry 2007 Jul 17;46(28):8263-72.
      doi: 10.1021/bi700623upubmed: 17580971google scholar: lookup
    86. DiCarlo CM, Vitello LB, Erman JE. Effect of active site and surface mutations on the reduction potential of yeast cytochrome c peroxidase and spectroscopic properties of the oxidized and reduced enzyme. J Inorg Biochem 2007 Apr;101(4):603-13.
      doi: 10.1016/j.jinorgbio.2006.12.006pubmed: 17275914google scholar: lookup
    87. Volkov AN, Worrall JA, Holtzmann E, Ubbink M. Solution structure and dynamics of the complex between cytochrome c and cytochrome c peroxidase determined by paramagnetic NMR. Proc Natl Acad Sci U S A 2006 Dec 12;103(50):18945-50.
      doi: 10.1073/pnas.0603551103pubmed: 17146057google scholar: lookup
    88. Nakani S, Vitello LB, Erman JE. Characterization of four covalently-linked yeast cytochrome c/cytochrome c peroxidase complexes: Evidence for electrostatic interaction between bound cytochrome c molecules. Biochemistry 2006 Dec 5;45(48):14371-8.
      doi: 10.1021/bi061662ppubmed: 17128976google scholar: lookup
    89. Talasaz AH, Nemat-Gorgani M, Liu Y, Ståhl P, Dutton RW, Ronaghi M, Davis RW. Prediction of protein orientation upon immobilization on biological and nonbiological surfaces. Proc Natl Acad Sci U S A 2006 Oct 3;103(40):14773-8.
      doi: 10.1073/pnas.0605841103pubmed: 17001006google scholar: lookup
    90. Ueno T, Yokoi N, Unno M, Matsui T, Tokita Y, Yamada M, Ikeda-Saito M, Nakajima H, Watanabe Y. Design of metal cofactors activated by a protein-protein electron transfer system. Proc Natl Acad Sci U S A 2006 Jun 20;103(25):9416-21.
      doi: 10.1073/pnas.0510968103pubmed: 16769893google scholar: lookup
    91. Millett F, Durham B. Kinetics of Electron Transfer within Cytochrome bc (1) and Between Cytochrome bc (1) and Cytochrome c. Photosynth Res 2004;82(1):1-16.
      doi: 10.1023/B:PRES.0000040434.77061.capubmed: 16228609google scholar: lookup
    92. Kang SA, Crane BR. Effects of interface mutations on association modes and electron-transfer rates between proteins. Proc Natl Acad Sci U S A 2005 Oct 25;102(43):15465-70.
      doi: 10.1073/pnas.0505176102pubmed: 16227441google scholar: lookup
    93. Bertini I, Cavallaro G, Rosato A. A structural model for the adduct between cytochrome c and cytochrome c oxidase. J Biol Inorg Chem 2005 Oct;10(6):613-24.
      doi: 10.1007/s00775-005-0011-7pubmed: 16151864google scholar: lookup
    94. Axelrod HL, Okamura MY. The structure and function of the cytochrome c2: reaction center electron transfer complex from Rhodobacter sphaeroides. Photosynth Res 2005;85(1):101-14.
      doi: 10.1007/s11120-005-1368-8pubmed: 15977062google scholar: lookup
    95. Hirota S, Okumura H, Kuroiwa S, Funasaki N, Watanabe Y. Reduction of ferricytochrome c by tyrosyltyrosylphenylalanine. J Biol Inorg Chem 2005 Jun;10(4):355-63.
      doi: 10.1007/s00775-005-0644-6pubmed: 15868183google scholar: lookup
    96. Hoffman BM, Celis LM, Cull DA, Patel AD, Seifert JL, Wheeler KE, Wang J, Yao J, Kurnikov IV, Nocek JM. Differential influence of dynamic processes on forward and reverse electron transfer across a protein-protein interface. Proc Natl Acad Sci U S A 2005 Mar 8;102(10):3564-9.
      doi: 10.1073/pnas.0408767102pubmed: 15738411google scholar: lookup
    97. Gray HB, Winkler JR. Long-range electron transfer. Proc Natl Acad Sci U S A 2005 Mar 8;102(10):3534-9.
      doi: 10.1073/pnas.0408029102pubmed: 15738403google scholar: lookup
    98. Guo M, Bhaskar B, Li H, Barrows TP, Poulos TL. Crystal structure and characterization of a cytochrome c peroxidase-cytochrome c site-specific cross-link. Proc Natl Acad Sci U S A 2004 Apr 20;101(16):5940-5.
      doi: 10.1073/pnas.0306708101pubmed: 15071191google scholar: lookup
    99. Ferrari D, Di Valentin M, Carbonera D, Merli A, Chen ZW, Mathews FS, Davidson VL, Rossi GL. Electron transfer in crystals of the binary and ternary complexes of methylamine dehydrogenase with amicyanin and cytochrome c551i as detected by EPR spectroscopy. J Biol Inorg Chem 2004 Mar;9(2):231-7.
      doi: 10.1007/s00775-003-0513-0pubmed: 14735334google scholar: lookup
    100. Banci L, Bertini I, Felli IC, Krippahl L, Kubicek K, Moura JJ, Rosato A. A further investigation of the cytochrome b5-cytochrome c complex. J Biol Inorg Chem 2003 Sep;8(7):777-86.
      doi: 10.1007/s00775-003-0479-ypubmed: 12884088google scholar: lookup
    101. Sivakolundu SG, Mabrouk PA. Structure-function relationship of reduced cytochrome c probed by complete solution structure determination in 30% acetonitrile/water solution. J Biol Inorg Chem 2003 May;8(5):527-539.
      doi: 10.1007/s00775-002-0437-0pubmed: 12764601google scholar: lookup
    102. Hays AM, Gray HB, Goodin DB. Trapping of peptide-based surrogates in an artificially created channel of cytochrome c peroxidase. Protein Sci 2003 Feb;12(2):278-87.
      doi: 10.1110/ps.0228403pubmed: 12538891google scholar: lookup
    103. Bamford VA, Bruno S, Rasmussen T, Appia-Ayme C, Cheesman MR, Berks BC, Hemmings AM. Structural basis for the oxidation of thiosulfate by a sulfur cycle enzyme. EMBO J 2002 Nov 1;21(21):5599-610.
      doi: 10.1093/emboj/cdf566pubmed: 12411478google scholar: lookup
    104. Fromme P, Bottin H, Krauss N, Sétif P. Crystallization and electron paramagnetic resonance characterization of the complex of photosystem I with its natural electron acceptor ferredoxin. Biophys J 2002 Oct;83(4):1760-73.
      doi: 10.1016/S0006-3495(02)73942-8pubmed: 12324399google scholar: lookup
    105. Rosenfeld RJ, Hays AM, Musah RA, Goodin DB. Excision of a proposed electron transfer pathway in cytochrome c peroxidase and its replacement by a ligand-binding channel. Protein Sci 2002 May;11(5):1251-9.
      doi: 10.1110/ps.4870102pubmed: 11967381google scholar: lookup
    106. Patel CN, Noble SM, Weatherly GT, Tripathy A, Winzor DJ, Pielak GJ. Effects of molecular crowding by saccharides on alpha-chymotrypsin dimerization. Protein Sci 2002 May;11(5):997-1003.
      doi: 10.1110/ps.4450102pubmed: 11967357google scholar: lookup
    107. Lange C, Hunte C. Crystal structure of the yeast cytochrome bc1 complex with its bound substrate cytochrome c. Proc Natl Acad Sci U S A 2002 Mar 5;99(5):2800-5.
      doi: 10.1073/pnas.052704699pubmed: 11880631google scholar: lookup
    108. Fritz G, Roth A, Schiffer A, Büchert T, Bourenkov G, Bartunik HD, Huber H, Stetter KO, Kroneck PM, Ermler U. Structure of adenylylsulfate reductase from the hyperthermophilic Archaeoglobus fulgidus at 1.6-A resolution. Proc Natl Acad Sci U S A 2002 Feb 19;99(4):1836-41.
      doi: 10.1073/pnas.042664399pubmed: 11842205google scholar: lookup
    109. Fernández-Recio J, Totrov M, Abagyan R. Soft protein-protein docking in internal coordinates. Protein Sci 2002 Feb;11(2):280-91.
      doi: 10.1110/ps.19202pubmed: 11790838google scholar: lookup
    110. Morelli XJ, Palma PN, Guerlesquin F, Rigby AC. A novel approach for assessing macromolecular complexes combining soft-docking calculations with NMR data. Protein Sci 2001 Oct;10(10):2131-7.
      doi: 10.1110/ps.07501pubmed: 11567104google scholar: lookup
    111. Taniuchi H, Shi Y, San Miguel GI, Ferretti JA, Mack JW, Fisher A, Shah M, Schechter AN, Shiloach J. A study of the influence of the hydrophobic core residues of yeast iso-2-cytochrome c on phosphate binding: a probe of the hydrophobic core-surface charge interactions. J Protein Chem 2001 Apr;20(3):203-15.
      doi: 10.1023/a:1010906929793pubmed: 11565900google scholar: lookup
    112. Tezcan FA, Crane BR, Winkler JR, Gray HB. Electron tunneling in protein crystals. Proc Natl Acad Sci U S A 2001 Apr 24;98(9):5002-6.
      doi: 10.1073/pnas.081072898pubmed: 11296248google scholar: lookup
    113. Morales R, Charon MH, Kachalova G, Serre L, Medina M, Gómez-Moreno C, Frey M. A redox-dependent interaction between two electron-transfer partners involved in photosynthesis. EMBO Rep 2000 Sep;1(3):271-6.
      doi: 10.1093/embo-reports/kvd057pubmed: 11256611google scholar: lookup
    114. Elcock AH, McCammon JA. Calculation of weak protein-protein interactions: the pH dependence of the second virial coefficient. Biophys J 2001 Feb;80(2):613-25.
      doi: 10.1016/S0006-3495(01)76042-0pubmed: 11159430google scholar: lookup
    115. Santana M, Pereira MM, Elias NP, Soares CM, Teixeira M. Gene cluster of Rhodothermus marinus high-potential iron-sulfur Protein: oxygen oxidoreductase, a caa(3)-type oxidase belonging to the superfamily of heme-copper oxidases. J Bacteriol 2001 Jan;183(2):687-99.
      doi: 10.1128/JB.183.2.687-699.2001pubmed: 11133964google scholar: lookup
    116. Kornblatt JA, Kornblatt MJ, Rajotte I, Hoa GH, Kahn PC. Thermodynamic volume cycles for electron transfer in the cytochrome c oxidase and for the binding of cytochrome c to cytochrome c oxidase. Biophys J 1998 Jul;75(1):435-44.
      doi: 10.1016/S0006-3495(98)77531-9pubmed: 9649404google scholar: lookup
    117. Moore GR, Cox MC, Crowe D, Osborne MJ, Rosell FI, Bujons J, Barker PD, Mauk MR, Mauk AG. N epsilon,N epsilon-dimethyl-lysine cytochrome c as an NMR probe for lysine involvement in protein-protein complex formation. Biochem J 1998 Jun 1;332 ( Pt 2)(Pt 2):439-49.
      doi: 10.1042/bj3320439pubmed: 9601073google scholar: lookup
    118. Cao Y, Musah RA, Wilcox SK, Goodin DB, McRee DE. Protein conformer selection by ligand binding observed with crystallography. Protein Sci 1998 Jan;7(1):72-8.
      doi: 10.1002/pro.5560070107pubmed: 9514261google scholar: lookup
    119. Hoover DM, Ludwig ML. A flavodoxin that is required for enzyme activation: the structure of oxidized flavodoxin from Escherichia coli at 1.8 A resolution. Protein Sci 1997 Dec;6(12):2525-37.
      doi: 10.1002/pro.5560061205pubmed: 9416602google scholar: lookup
    120. Gazaryan IG, Klyachko NL, Dulkis YK, Ouporov IV, Levashov AV. Formation and properties of dimeric recombinant horseradish peroxidase in a system of reversed micelles. Biochem J 1997 Dec 1;328 ( Pt 2)(Pt 2):643-7.
      doi: 10.1042/bj3280643pubmed: 9371726google scholar: lookup
    121. Fetrow JS, Horner SR, Oehrl W, Schaak DL, Boose TL, Burton RE. Analysis of the structure and stability of omega loop A replacements in yeast iso-1-cytochrome c. Protein Sci 1997 Jan;6(1):197-210.
      doi: 10.1002/pro.5560060122pubmed: 9007992google scholar: lookup
    122. Millett F, Miller MA, Geren L, Durham B. Electron transfer between cytochrome c and cytochrome c peroxidase. J Bioenerg Biomembr 1995 Jun;27(3):341-51.
      doi: 10.1007/BF02110103pubmed: 8847347google scholar: lookup
    123. Mauk AG, Mauk MR, Moore GR, Northrup SH. Experimental and theoretical analysis of the interaction between cytochrome c and cytochrome b5. J Bioenerg Biomembr 1995 Jun;27(3):311-30.
      doi: 10.1007/BF02110101pubmed: 8847345google scholar: lookup
    124. Curry WB, Grabe MD, Kurnikov IV, Skourtis SS, Beratan DN, Regan JJ, Aquino AJ, Beroza P, Onuchic JN. Pathways, pathway tubes, pathway docking, and propagators in electron transfer proteins. J Bioenerg Biomembr 1995 Jun;27(3):285-93.
      doi: 10.1007/BF02110098pubmed: 8847342google scholar: lookup
    125. Moser CC, Page CC, Farid R, Dutton PL. Biological electron transfer. J Bioenerg Biomembr 1995 Jun;27(3):263-74.
      doi: 10.1007/BF02110096pubmed: 8847340google scholar: lookup
    126. Musser JM. Antimicrobial agent resistance in mycobacteria: molecular genetic insights. Clin Microbiol Rev 1995 Oct;8(4):496-514.
      doi: 10.1128/CMR.8.4.496pubmed: 8665467google scholar: lookup
    127. Kornblatt JA, Kornblatt MJ, Hoa GH, Mauk AG. Responses of two protein-protein complexes to solvent stress: does water play a role at the interface?. Biophys J 1993 Sep;65(3):1059-65.
      doi: 10.1016/S0006-3495(93)81168-8pubmed: 8241386google scholar: lookup
    128. Zhou HX. Boundary element solution of macromolecular electrostatics: interaction energy between two proteins. Biophys J 1993 Aug;65(2):955-63.
      doi: 10.1016/S0006-3495(93)81094-4pubmed: 8218918google scholar: lookup
    129. De Pascalis AR, Jelesarov I, Ackermann F, Koppenol WH, Hirasawa M, Knaff DB, Bosshard HR. Binding of ferredoxin to ferredoxin:NADP+ oxidoreductase: the role of carboxyl groups, electrostatic surface potential, and molecular dipole moment. Protein Sci 1993 Jul;2(7):1126-35.
      doi: 10.1002/pro.5560020707pubmed: 8102922google scholar: lookup
    130. Miller MA, Han GW, Kraut J. A cation binding motif stabilizes the compound I radical of cytochrome c peroxidase. Proc Natl Acad Sci U S A 1994 Nov 8;91(23):11118-22.
      doi: 10.1073/pnas.91.23.11118pubmed: 7972020google scholar: lookup
    131. Lo TP, Murphy ME, Guillemette JG, Smith M, Brayer GD. Replacements in a conserved leucine cluster in the hydrophobic heme pocket of cytochrome c. Protein Sci 1995 Feb;4(2):198-208.
      doi: 10.1002/pro.5560040207pubmed: 7757009google scholar: lookup
    132. Shin DW, Zhong F, Pletneva EV. Differences in functional cross-talk between loops C and D in two mitochondrial cytochromes. J Inorg Biochem 2026 Mar;276:113182.
      doi: 10.1016/j.jinorgbio.2025.113182pubmed: 41411686google scholar: lookup
    133. Gong R, Qu Y, Liu J, Zhang X, Zhou L, Tian Z, Zeng X, Jin B, Li Z, Yu L, Chen R, Zhou Y, Liao L, Yang L, Song X, Cai YS, Shen K, Deng Z, Zhang Z, Wang B, Chen W. A two-metalloenzyme cascade constructs the azetidine-containing pharmacophore. Nat Chem 2026 Mar;18(3):482-491.
      doi: 10.1038/s41557-025-01949-ypubmed: 41028918google scholar: lookup
    134. Tobin EE, Collins JH, Marsan CB, Nadeau GT, Mori K, Lipzen A, Mondo S, Grigoriev IV, Young EM. Omics-driven onboarding of the carotenoid producing red yeast Xanthophyllomyces dendrorhous CBS 6938. Appl Microbiol Biotechnol 2024 Dec 28;108(1):547.
      doi: 10.1007/s00253-024-13379-wpubmed: 39731599google scholar: lookup
    135. Kwon H, Basran J, Pathak C, Hussain M, Freeman SL, Fielding AJ, Bailey AJ, Stefanou N, Sparkes HA, Tosha T, Yamashita K, Hirata K, Murakami H, Ueno G, Ago H, Tono K, Yamamoto M, Sawai H, Shiro Y, Sugimoto H, Raven EL, Moody PCE. XFEL Crystal Structures of Peroxidase Compound II. Angew Chem Weinheim Bergstr Ger 2021 Jun 21;133(26):14699-14706.
      doi: 10.1002/ange.202103010pubmed: 38505375google scholar: lookup
    136. Xin J, Min Z, Yu L, Yuan X, Liu A, Wu W, Zhang X, He H, Wu J, Xin Y, Blankenship RE, Tian C, Xu X. Cryo-EM structure of HQNO-bound alternative complex III from the anoxygenic phototrophic bacterium Chloroflexus aurantiacus. Plant Cell 2024 Oct 3;36(10):4212-4233.
      doi: 10.1093/plcell/koae029pubmed: 38299372google scholar: lookup
    137. Chertkova RV, Oleynikov IP, Pakhomov AA, Sudakov RV, Orlov VN, Semenova MA, Arutyunyan AM, Ptushenko VV, Kirpichnikov MP, Dolgikh DA, Vygodina TV. Mutant Cytochrome C as a Potential Detector of Superoxide Generation: Effect of Mutations on the Function and Properties. Cells 2023 Sep 19;12(18).
      doi: 10.3390/cells12182316pubmed: 37759538google scholar: lookup
    138. Yu L, Min Z, Liu M, Xin Y, Liu A, Kuang J, Wu W, Wu J, He H, Xin J, Blankenship RE, Tian C, Xu X. A cytochrome c(551) mediates the cyclic electron transport chain of the anoxygenic phototrophic bacterium Roseiflexus castenholzii. Plant Commun 2024 Feb 12;5(2):100715.
      doi: 10.1016/j.xplc.2023.100715pubmed: 37710959google scholar: lookup
    139. Freeman SL, Skafar V, Kwon H, Fielding AJ, Moody PCE, Martínez A, Issoglio FM, Inchausti L, Smircich P, Zeida A, Piacenza L, Radi R, Raven EL. Crystal structure of Trypanosoma cruzi heme peroxidase and characterization of its substrate specificity and compound I intermediate. J Biol Chem 2022 Aug;298(8):102204.
      doi: 10.1016/j.jbc.2022.102204pubmed: 35772495google scholar: lookup
    140. Owens CP, Katz FE, Carter CH, Luca MA, Tezcan FA. Evidence for Functionally Relevant Encounter Complexes in Nitrogenase Catalysis. J Am Chem Soc 2015 Oct 7;137(39):12704-12.
      doi: 10.1021/jacs.5b08310pubmed: 26360912google scholar: lookup
    Subscribe to our newsletter
    Join 99,658 horse owners like you who receive our email updates on horse health and nutrition.