Analyze Diet
The Journal of biological chemistry1979; 254(23); 11973-11981;

Comparison of yeast and beef cytochrome c oxidases. Kinetics and binding of horse, fungal, and Euglena cytochromes c.

Abstract: No abstract available
Publication Date: 1979-12-10 PubMed ID: 227884
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.
  • Comparative Study
  • Journal Article
  • Research Support
  • U.S. Gov't
  • Non-P.H.S.
  • Research Support
  • U.S. Gov't
  • P.H.S.

Cite This Article

APA
Dethmers JK, Ferguson-Miller S, Margoliash E. (1979). Comparison of yeast and beef cytochrome c oxidases. Kinetics and binding of horse, fungal, and Euglena cytochromes c. J Biol Chem, 254(23), 11973-11981.

Publication

ISSN: 0021-9258
NlmUniqueID: 2985121R
Country: United States
Language: English
Volume: 254
Issue: 23
Pages: 11973-11981

Researcher Affiliations

Dethmers, J K
    Ferguson-Miller, S
      Margoliash, E

        MeSH Terms

        • Amino Acid Sequence
        • Animals
        • Candida
        • Cattle
        • Cytochrome c Group
        • Electron Transport Complex IV / metabolism
        • Euglena
        • Horses
        • Kinetics
        • Mitochondria / enzymology
        • Mitochondria, Heart / enzymology
        • Models, Molecular
        • Neurospora crassa
        • Protein Binding
        • Protein Conformation
        • Saccharomyces cerevisiae / enzymology
        • Species Specificity
        • Tuna

        Citations

        This article has been cited 8 times.
        1. Brzezinski P, Moe A, Ädelroth P. Structure and Mechanism of Respiratory III-IV Supercomplexes in Bioenergetic Membranes. Chem Rev 2021 Aug 11;121(15):9644-9673.
          doi: 10.1021/acs.chemrev.1c00140pubmed: 34184881google scholar: lookup
        2. Zhou S, Pettersson P, Björck ML, Dawitz H, Brzezinski P, Mäler L, Ädelroth P. NMR structural analysis of the yeast cytochrome c oxidase subunit Cox13 and its interaction with ATP. BMC Biol 2021 May 10;19(1):98.
          doi: 10.1186/s12915-021-01036-xpubmed: 33971868google scholar: lookup
        3. Moe A, Di Trani J, Rubinstein JL, Brzezinski P. Cryo-EM structure and kinetics reveal electron transfer by 2D diffusion of cytochrome c in the yeast III-IV respiratory supercomplex. Proc Natl Acad Sci U S A 2021 Mar 16;118(11).
          doi: 10.1073/pnas.2021157118pubmed: 33836592google scholar: lookup
        4. 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
        5. Abdullaev ZKh, Bodrova ME, Chernyak BV, Dolgikh DA, Kluck RM, Pereverzev MO, Arseniev AS, Efremov RG, Kirpichnikov MP, Mokhova EN, Newmeyer DD, Roder H, Skulachev VP. A cytochrome c mutant with high electron transfer and antioxidant activities but devoid of apoptogenic effect. Biochem J 2002 Mar 15;362(Pt 3):749-54.
          doi: 10.1042/0264-6021:3620749pubmed: 11879204google scholar: lookup
        6. Diggens RJ, Ragan CI. Properties of ubiquinol oxidase reconstituted from ubiquinol-cytochrome c reductase, cytochrome c and cytochrome c oxidase. Biochem J 1982 Feb 15;202(2):527-34.
          doi: 10.1042/bj2020527pubmed: 6284131google scholar: lookup
        7. Osheroff N, Brautigan DL, Margoliash E. Mapping of anion binding sites on cytochrome c by differential chemical modification of lysine residues. Proc Natl Acad Sci U S A 1980 Aug;77(8):4439-43.
          doi: 10.1073/pnas.77.8.4439pubmed: 6254024google scholar: lookup
        8. Corthésy BE, Wallace CJ. The oxidation-state-dependent ATP-binding site of cytochrome c. A possible physiological significance. Biochem J 1986 Jun 1;236(2):359-64.
          doi: 10.1042/bj2360359pubmed: 3019313google scholar: lookup