FREE SHIPPING over $40
OVER 9000 FIVE-STAR REVIEWS
5% OFF ALL SUBSCRIPTIONS
100% HAPPINESS GUARANTEE
Analyze Diet
0
Home / Equine Research Bank / Chem Commun (Camb) / Direct observation of myoglobin structural dynamics from 100...
Chemical communications (Cambridge, England)2010; 47(1); 289-291; doi: 10.1039/c0cc01817a

Direct observation of myoglobin structural dynamics from 100 picoseconds to 1 microsecond with picosecond X-ray solution scattering.

Abstract: Here we report structural dynamics of equine myoglobin (Mb) in response to the CO photodissociation visualized by picosecond time-resolved X-ray solution scattering. The data clearly reveal new structural dynamics that occur in the timescale of ∼360 picoseconds (ps) and ∼9 nanoseconds (ns), which have not been clearly detected in previous studies.
Get Full Text
Publication Date: 2010-08-24 PubMed ID: 20733999PubMed Central: PMC2999690DOI: 10.1039/c0cc01817aGoogle 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
  • N.I.H.
  • Extramural
  • Research Support
  • Non-U.S. Gov't

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.

This research paper investigates the structural dynamics of myoglobin, a type of protein in muscle tissues, in response to carbon monoxide photodissociation, using a technique known as picosecond time-resolved X-ray solution scattering. The study finds new structural changes in the protein on the picosecond and nanosecond timescales that were not identified in prior research.

Introduction and Methodology

  • The research focuses on understanding the structural dynamics of equine myoglobin, an oxygen-binding protein present in horse muscle tissues. Myoglobin’s function relates to oxygen storage and delivery in muscles.
  • The investigation is triggered by carbon monoxide photodissociation – essentially the breaking down of carbon monoxide molecules using light.
  • To visualize these dynamics, the researchers use a technique known as picosecond time-resolved X-ray solution scattering. This advanced method allows for observations of structural changes in molecules on extremely short time scales – up to one trillionth (picosecond) of a second.

Results: Novel Structural Dynamics

  • The key findings of this research are new structural dynamics, or changes, within the myoglobin on timescales of approximately 360 picoseconds and 9 nanoseconds.
  • These timescales are incredibly short, with one picosecond being a trillionth of a second and a nanosecond being a billionth of a second. The detection of changes on these scales demonstrates the sensitivity of the picosecond X-ray solution scattering technique.
  • Such rapid structural changes had not been clearly detected in previous myoglobin studies, underscoring the novelty of these findings.

Implications of the Research

  • This novel observation can potentially contribute to the broader understanding of protein dynamics in general and the specific function and behavior of myoglobin.
  • Given the instrumental role of myoglobin in oxygen storage and delivery in muscles, insights from this research may have potential implications in muscular disease study, sports science, and other related areas.
  • More broadly, the demonstration of the picosecond time-resolved X-ray solution scattering technique’s effectiveness in identifying subtle and rapid changes at molecular level can promote its application in various other areas of scientific research.

Cite This Article

APA
Kim KH, Oang KY, Kim J, Lee JH, Kim Y, Ihee H. (2010). Direct observation of myoglobin structural dynamics from 100 picoseconds to 1 microsecond with picosecond X-ray solution scattering. Chem Commun (Camb), 47(1), 289-291. https://doi.org/10.1039/c0cc01817a

Publication

Chemical communications (Cambridge, England)
ISSN: 1364-548X
NlmUniqueID: 9610838
Country: England
Language: English
Volume: 47
Issue: 1
Pages: 289-291

Researcher Affiliations

Kim, Kyung Hwan
  • Center for Time-Resolved Diffraction, Department of Chemistry, Graduate School of Nanoscience & Technology (WCU), KAIST, Daejeon 305-701, Korea.
Oang, Key Young
    Kim, Jeongho
      Lee, Jae Hyuk
        Kim, Youngmin
          Ihee, Hyotcherl

            MeSH Terms

            • Carbon Monoxide / chemistry
            • Myoglobin / chemistry
            • Photochemistry
            • Protein Conformation
            • Scattering, Small Angle
            • Solutions
            • Thermodynamics
            • Time Factors
            • X-Ray Diffraction

            Grant Funding

            • P41 RR007707 / NCRR NIH HHS
            • P41 RR007707-12 / NCRR NIH HHS
            • RR007707 / NCRR NIH HHS

            References

            This article includes 29 references
            1. Beece D, Eisenstein L, Frauenfelder H, Good D, Marden MC, Reinisch L, Reynolds AH, Sorensen LB, Yue KT. Solvent viscosity and protein dynamics.. Biochemistry 1980 Nov 11;19(23):5147-57.
              pubmed: 7448161doi: 10.1021/bi00564a001google scholar: lookup
            2. Franzen S, Bohn B, Poyart C, Martin JL. Evidence for sub-picosecond heme doming in hemoglobin and myoglobin: a time-resolved resonance Raman comparison of carbonmonoxy and deoxy species.. Biochemistry 1995 Jan 31;34(4):1224-37.
              pubmed: 7827072doi: 10.1021/bi00004a016google scholar: lookup
            3. Richard L, Genberg L, Deak J, Chiu HL, Miller RJ. Picosecond phase grating spectroscopy of hemoglobin and myoglobin: energetics and dynamics of global protein motion.. Biochemistry 1992 Nov 10;31(44):10703-15.
              pubmed: 1420186doi: 10.1021/bi00159a010google scholar: lookup
            4. Dadusc G, Ogilvie JP, Schulenberg P, Marvet U, Miller RJ. Diffractive optics-based heterodyne-detected four-wave mixing signals of protein motion: from "protein quakes" to ligand escape for myoglobin.. Proc Natl Acad Sci U S A 2001 May 22;98(11):6110-5.
              pmc: PMC33430pubmed: 11344263doi: 10.1073/pnas.101130298google scholar: lookup
            5. Sato A, Mizutani Y. Picosecond structural dynamics of myoglobin following photodissociation of carbon monoxide as revealed by ultraviolet time-resolved resonance Raman spectroscopy.. Biochemistry 2005 Nov 15;44(45):14709-14.
              pubmed: 16274218doi: 10.1021/bi051732cgoogle scholar: lookup
            6. Xie XL, Simon JD. Protein conformational relaxation following photodissociation of CO from carbonmonoxymyoglobin: picosecond circular dichroism and absorption studies.. Biochemistry 1991 Apr 16;30(15):3682-92.
              pubmed: 2015224doi: 10.1021/bi00229a013google scholar: lookup
            7. Sakakura M, Yamaguchi S, Hirota N, Terazima M. Dynamics of structure and energy of horse carboxymyoglobin after photodissociation of carbon monoxide.. J Am Chem Soc 2001 May 9;123(18):4286-94.
              pubmed: 11457195doi: 10.1021/ja9944655google scholar: lookup
            8. Zhang L, Wang L, Kao YT, Qiu W, Yang Y, Okobiah O, Zhong D. Mapping hydration dynamics around a protein surface.. Proc Natl Acad Sci U S A 2007 Nov 20;104(47):18461-6.
              pmc: PMC2141799pubmed: 18003912doi: 10.1073/pnas.0707647104google scholar: lookup
            9. Schmidt M, Nienhaus K, Pahl R, Krasselt A, Anderson S, Parak F, Nienhaus GU, Srajer V. Ligand migration pathway and protein dynamics in myoglobin: a time-resolved crystallographic study on L29W MbCO.. Proc Natl Acad Sci U S A 2005 Aug 16;102(33):11704-9.
              pmc: PMC1187994pubmed: 16085709doi: 10.1073/pnas.0504932102google scholar: lookup
            10. Bourgeois D, Vallone B, Schotte F, Arcovito A, Miele AE, Sciara G, Wulff M, Anfinrud P, Brunori M. Complex landscape of protein structural dynamics unveiled by nanosecond Laue crystallography.. Proc Natl Acad Sci U S A 2003 Jul 22;100(15):8704-9.
              pmc: PMC166376pubmed: 12847289doi: 10.1073/pnas.1430900100google scholar: lookup
            11. Ostermann A, Waschipky R, Parak FG, Nienhaus GU. Ligand binding and conformational motions in myoglobin.. Nature 2000 Mar 9;404(6774):205-8.
              pubmed: 10724176doi: 10.1038/35004622google scholar: lookup
            12. Srajer V, Teng T, Ursby T, Pradervand C, Ren Z, Adachi S, Schildkamp W, Bourgeois D, Wulff M, Moffat K. Photolysis of the carbon monoxide complex of myoglobin: nanosecond time-resolved crystallography.. Science 1996 Dec 6;274(5293):1726-9.
              pubmed: 8939867doi: 10.1126/science.274.5293.1726google scholar: lookup
            13. Schotte F, Lim M, Jackson TA, Smirnov AV, Soman J, Olson JS, Phillips GN Jr, Wulff M, Anfinrud PA. Watching a protein as it functions with 150-ps time-resolved x-ray crystallography.. Science 2003 Jun 20;300(5627):1944-7.
              pubmed: 12817148doi: 10.1126/science.1078797google scholar: lookup
            14. Quillin ML, Li T, Olson JS, Phillips GN Jr, Dou Y, Ikeda-Saito M, Regan R, Carlson M, Gibson QH, Li H. Structural and functional effects of apolar mutations of the distal valine in myoglobin.. J Mol Biol 1995 Jan 27;245(4):416-36.
              pubmed: 7837273doi: 10.1006/jmbi.1994.0034google scholar: lookup
            15. Aranda R 4th, Levin EJ, Schotte F, Anfinrud PA, Phillips GN Jr. Time-dependent atomic coordinates for the dissociation of carbon monoxide from myoglobin.. Acta Crystallogr D Biol Crystallogr 2006 Jul;62(Pt 7):776-83.
              pubmed: 16790933doi: 10.1107/S0907444906017318google scholar: lookup
            16. Chu K, Vojtchovský J, McMahon BH, Sweet RM, Berendzen J, Schlichting I. Structure of a ligand-binding intermediate in wild-type carbonmonoxy myoglobin.. Nature 2000 Feb 24;403(6772):921-3.
              pubmed: 10706294doi: 10.1038/35002641google scholar: lookup
            17. Ejdrup T, Lemke HT, Haldrup K, Nielsen TN, Arms DA, Walko DA, Miceli A, Landahl EC, Dufresne EM, Nielsen MM. Picosecond time-resolved laser pump/X-ray probe experiments using a gated single-photon-counting area detector.. J Synchrotron Radiat 2009 May;16(Pt 3):387-90.
              pubmed: 19395803doi: 10.1107/S0909049509004658google scholar: lookup
            18. Ihee H. Visualizing solution-phase reaction dynamics with time-resolved X-ray liquidography.. Acc Chem Res 2009 Feb 17;42(2):356-66.
              pubmed: 19117426doi: 10.1021/ar800168vgoogle scholar: lookup
            19. Vincent J, Andersson M, Eklund M, Wöhri AB, Odelius M, Malmerberg E, Kong Q, Wulff M, Neutze R, Davidsson J. Solvent dependent structural perturbations of chemical reaction intermediates visualized by time-resolved x-ray diffraction.. J Chem Phys 2009 Apr 21;130(15):154502.
              pubmed: 19388754doi: 10.1063/1.3111401google scholar: lookup
            20. Moffat K. Time-resolved biochemical crystallography: a mechanistic perspective.. Chem Rev 2001 Jun;101(6):1569-81.
              pubmed: 11709992doi: 10.1021/cr990039qgoogle scholar: lookup
            21. Chergui M, Zewail AH. Electron and X-ray methods of ultrafast structural dynamics: advances and applications.. Chemphyschem 2009 Jan 12;10(1):28-43.
              pubmed: 19130540doi: 10.1002/cphc.200800667google scholar: lookup
            22. Cammarata M, Levantino M, Schotte F, Anfinrud PA, Ewald F, Choi J, Cupane A, Wulff M, Ihee H. Tracking the structural dynamics of proteins in solution using time-resolved wide-angle X-ray scattering.. Nat Methods 2008 Oct;5(10):881-6.
              pmc: PMC3159148pubmed: 18806790doi: 10.1038/nmeth.1255google scholar: lookup
            23. Ahn S, Kim KH, Kim Y, Kim J, Ihee H. Protein tertiary structural changes visualized by time-resolved X-ray solution scattering.. J Phys Chem B 2009 Oct 8;113(40):13131-3.
              pubmed: 19757799doi: 10.1021/jp906983vgoogle scholar: lookup
            24. Andersson M, Malmerberg E, Westenhoff S, Katona G, Cammarata M, Wöhri AB, Johansson LC, Ewald F, Eklund M, Wulff M, Davidsson J, Neutze R. Structural dynamics of light-driven proton pumps.. Structure 2009 Sep 9;17(9):1265-75.
              pubmed: 19748347doi: 10.1016/j.str.2009.07.007google scholar: lookup
            25. Cho HS, Dashdorj N, Schotte F, Graber T, Henning R, Anfinrud P. Protein structural dynamics in solution unveiled via 100-ps time-resolved x-ray scattering.. Proc Natl Acad Sci U S A 2010 Apr 20;107(16):7281-6.
              pmc: PMC2867760pubmed: 20406909doi: 10.1073/pnas.1002951107google scholar: lookup
            26. Richard L, Genberg L, Deak J, Chiu HL, Miller RJ. Picosecond phase grating spectroscopy of hemoglobin and myoglobin: energetics and dynamics of global protein motion.. Biochemistry 1992 Nov 10;31(44):10703-15.
              pubmed: 1420186doi: 10.1021/bi00159a010google scholar: lookup
            27. Sakakura M, Yamaguchi S, Hirota N, Terazima M. Dynamics of structure and energy of horse carboxymyoglobin after photodissociation of carbon monoxide.. J Am Chem Soc 2001 May 9;123(18):4286-94.
              pubmed: 11457195doi: 10.1021/ja9944655google scholar: lookup
            28. Henry ER, Sommer JH, Hofrichter J, Eaton WA. Geminate recombination of carbon monoxide to myoglobin.. J Mol Biol 1983 May 25;166(3):443-51.
              pubmed: 6854651doi: 10.1016/s0022-2836(83)80094-1google scholar: lookup
            29. Dartigalongue T, Niezborala C, Hache F. Subpicosecond UV spectroscopy of carbonmonoxy-myoglobin: absorption and circular dichroism studies.. Phys Chem Chem Phys 2007 Apr 7;9(13):1611-5.
              pubmed: 17429554doi: 10.1039/b616173agoogle scholar: lookup

            Citations

            This article has been cited 19 times.
            1. Kosheleva I, Henning R, Kim I, Kim SO, Kusel M, Srajer V. Sample-minimizing co-flow cell for time-resolved pump-probe X-ray solution scattering. J Synchrotron Radiat 2023 Mar 1;30(Pt 2):490-499.
              doi: 10.1107/S1600577522012127pubmed: 36891863google scholar: lookup
            2. Sarabi D, Ostojić L, Bosman R, Vallejos A, Linse JB, Wulff M, Levantino M, Neutze R. Modeling difference x-ray scattering observations from an integral membrane protein within a detergent micelle. Struct Dyn 2022 Sep;9(5):054102.
              doi: 10.1063/4.0000157pubmed: 36329868google scholar: lookup
            3. Gu J, Lee S, Eom S, Ki H, Choi EH, Lee Y, Nozawa S, Adachi SI, Kim J, Ihee H. Structural Dynamics of C(2)F(4)I(2) in Cyclohexane Studied via Time-Resolved X-ray Liquidography. Int J Mol Sci 2021 Sep 10;22(18).
              doi: 10.3390/ijms22189793pubmed: 34575954google scholar: lookup
            4. Choi M, Kim JG, Muniyappan S, Kim H, Kim TW, Lee Y, Lee SJ, Kim SO, Ihee H. Effect of the abolition of intersubunit salt bridges on allosteric protein structural dynamics. Chem Sci 2021 May 10;12(23):8207-8217.
              doi: 10.1039/d1sc01207jpubmed: 34194711google scholar: lookup
            5. Ki H, Park S, Eom S, Gu J, Kim S, Kim C, Ahn CW, Choi M, Ahn S, Ahn DS, Choi J, Baik MH, Ihee H. Gold Nanoparticle Formation via X-ray Radiolysis Investigated with Time-Resolved X-ray Liquidography. Int J Mol Sci 2020 Sep 27;21(19).
              doi: 10.3390/ijms21197125pubmed: 32992497google scholar: lookup
            6. Yang C, Choi M, Kim JG, Kim H, Muniyappan S, Nozawa S, Adachi SI, Henning R, Kosheleva I, Ihee H. Protein Structural Dynamics of Wild-Type and Mutant Homodimeric Hemoglobin Studied by Time-Resolved X-Ray Solution Scattering. Int J Mol Sci 2018 Nov 18;19(11).
              doi: 10.3390/ijms19113633pubmed: 30453670google scholar: lookup
            7. Rimmerman D, Leshchev D, Hsu DJ, Hong J, Abraham B, Henning R, Kosheleva I, Chen LX. Probing Cytochrome c Folding Transitions upon Phototriggered Environmental Perturbations Using Time-Resolved X-ray Scattering. J Phys Chem B 2018 May 24;122(20):5218-5224.
              doi: 10.1021/acs.jpcb.8b03354pubmed: 29709179google scholar: lookup
            8. Rimmerman D, Leshchev D, Hsu DJ, Hong J, Kosheleva I, Chen LX. Direct Observation of Insulin Association Dynamics with Time-Resolved X-ray Scattering. J Phys Chem Lett 2017 Sep 21;8(18):4413-4418.
              doi: 10.1021/acs.jpclett.7b01720pubmed: 28853898google scholar: lookup
            9. Oang KY, Yang C, Muniyappan S, Kim J, Ihee H. SVD-aided pseudo principal-component analysis: A new method to speed up and improve determination of the optimum kinetic model from time-resolved data. Struct Dyn 2017 Jul;4(4):044013.
              doi: 10.1063/1.4979854pubmed: 28405591google scholar: lookup
            10. Brinkmann LU, Hub JS. Ultrafast anisotropic protein quake propagation after CO photodissociation in myoglobin. Proc Natl Acad Sci U S A 2016 Sep 20;113(38):10565-70.
              doi: 10.1073/pnas.1603539113pubmed: 27601659google scholar: lookup
            11. Silatani M, Lima FA, Penfold TJ, Rittmann J, Reinhard ME, Rittmann-Frank HM, Borca C, Grolimund D, Milne CJ, Chergui M. NO binding kinetics in myoglobin investigated by picosecond Fe K-edge absorption spectroscopy. Proc Natl Acad Sci U S A 2015 Oct 20;112(42):12922-7.
              doi: 10.1073/pnas.1424446112pubmed: 26438842google scholar: lookup
            12. Oang KY, Kim KH, Jo J, Kim Y, Kim JG, Kim TW, Jun S, Kim J, Ihee H. Sub-100-ps structural dynamics of horse heart myoglobin probed by time-resolved X-ray solution scattering. Chem Phys 2014 Oct 17;422:137-142.
              doi: 10.1016/j.chemphys.2014.03.004pubmed: 25678733google scholar: lookup
            13. Chen PC, Hub JS. Validating solution ensembles from molecular dynamics simulation by wide-angle X-ray scattering data. Biophys J 2014 Jul 15;107(2):435-447.
              doi: 10.1016/j.bpj.2014.06.006pubmed: 25028885google scholar: lookup
            14. Neutze R. Opportunities and challenges for time-resolved studies of protein structural dynamics at X-ray free-electron lasers. Philos Trans R Soc Lond B Biol Sci 2014 Jul 17;369(1647):20130318.
              doi: 10.1098/rstb.2013.0318pubmed: 24914150google scholar: lookup
            15. Oang KY, Kim JG, Yang C, Kim TW, Kim Y, Kim KH, Kim J, Ihee H. Conformational Substates of Myoglobin Intermediate Resolved by Picosecond X-ray Solution Scattering. J Phys Chem Lett 2014 Mar 6;5(5):804-808.
              doi: 10.1021/jz4027425pubmed: 24761190google scholar: lookup
            16. Neutze R, Moffat K. Time-resolved structural studies at synchrotrons and X-ray free electron lasers: opportunities and challenges. Curr Opin Struct Biol 2012 Oct;22(5):651-9.
              doi: 10.1016/j.sbi.2012.08.006pubmed: 23021004google scholar: lookup
            17. Kim KH, Muniyappan S, Oang KY, Kim JG, Nozawa S, Sato T, Koshihara SY, Henning R, Kosheleva I, Ki H, Kim Y, Kim TW, Kim J, Adachi S, Ihee H. Direct observation of cooperative protein structural dynamics of homodimeric hemoglobin from 100 ps to 10 ms with pump-probe X-ray solution scattering. J Am Chem Soc 2012 Apr 25;134(16):7001-8.
              doi: 10.1021/ja210856vpubmed: 22494177google scholar: lookup
            18. Kim J, Kim KH, Kim JG, Kim TW, Kim Y, Ihee H. Anisotropic Picosecond X-ray Solution Scattering from Photo-selectively Aligned Protein Molecules. J Phys Chem Lett 2011 Feb 2;2(5):350-356.
              doi: 10.1021/jz101503rpubmed: 21643489google scholar: lookup
            19. Henning RW, Kosheleva I, Šrajer V, Kim IS, Zoellner E, Ranganathan R. BioCARS: Synchrotron facility for probing structural dynamics of biological macromolecules. Struct Dyn 2024 Jan;11(1):014301.
              doi: 10.1063/4.0000238pubmed: 38304444google scholar: lookup
            Subscribe to our newsletter
            Join 99,383 horse owners like you who receive our email updates on horse health and nutrition.