Literature DB >> 8389744

The sequence of electron carriers in the reaction of cytochrome c oxidase with oxygen.

B C Hill1.   

Abstract

Kinetic studies of the electron transfer processes performed by cytochrome oxidase have assigned rates of electron transfer between the metal centers involved in the oxidation of ferrocytochrome c by molecular oxygen. Transient-state studies of the reaction with oxygen have led to the proposal of a sequence of carriers from cytochrome c, to CuA, to cytochrome a, and then to the binuclear (i.e., cytochrome a3-CuB) center. Electron exchange rates between these centers agree with relative center-to-center distances as follows; cytochrome c to CuA 5-7 A, cytochrome c to cytochrome a 20-25 A, CuA to cytochrome a 14-16 A and cytochrome a to cytochrome a3-CuB 8-10 A. It is proposed that the step from cytochrome a to the binuclear center is the key control point in the reaction and that this step is one of the major points of energy transduction in the reaction cycle.

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Year:  1993        PMID: 8389744     DOI: 10.1007/bf00762853

Source DB:  PubMed          Journal:  J Bioenerg Biomembr        ISSN: 0145-479X            Impact factor:   2.945


  32 in total

1.  Photochemical and ligand-exchange properties of the cyanide complex of fully reduced cytochrome c oxidase.

Authors:  B C Hill; S Marmor
Journal:  Biochem J       Date:  1991-10-15       Impact factor: 3.857

2.  A nontraditional role for water in the cytochrome c oxidase reaction.

Authors:  J A Kornblatt; G H Hoa
Journal:  Biochemistry       Date:  1990-10-09       Impact factor: 3.162

3.  Binding of ligands and spectral shifts in cytochrome c oxidase.

Authors:  P Nicholls; V Hildebrandt
Journal:  Biochem J       Date:  1978-07-01       Impact factor: 3.857

4.  The reaction of the electrostatic cytochrome c-cytochrome oxidase complex with oxygen.

Authors:  B C Hill
Journal:  J Biol Chem       Date:  1991-02-05       Impact factor: 5.157

5.  Nature and functional implications of the cytochrome a3 transients after photodissociation of CO-cytochrome oxidase.

Authors:  W H Woodruff; O Einarsdóttir; R B Dyer; K A Bagley; G Palmer; S J Atherton; R A Goldbeck; T D Dawes; D S Kliger
Journal:  Proc Natl Acad Sci U S A       Date:  1991-03-15       Impact factor: 11.205

6.  The reaction of fully reduced cytochrome c oxidase with oxygen studied by flow-flash spectrophotometry at room temperature. Evidence for new pathways of electron transfer.

Authors:  B C Hill; C Greenwood
Journal:  Biochem J       Date:  1984-03-15       Impact factor: 3.857

7.  Formation and decay of the primary oxygen compound of cytochrome oxidase at room temperature as observed by stopped flow, laser flash photolysis and rapid scanning.

Authors:  Y Orii
Journal:  J Biol Chem       Date:  1984-06-10       Impact factor: 5.157

8.  Flow-flash, time-resolved resonance Raman spectroscopy of the oxidation of reduced and of mixed valence cytochrome oxidase by dioxygen.

Authors:  G T Babcock; J M Jean; L N Johnston; W H Woodruff; G Palmer
Journal:  J Inorg Biochem       Date:  1985 Mar-Apr       Impact factor: 4.155

9.  Definition of the catalytic site of cytochrome c oxidase: specific ligands of heme a and the heme a3-CuB center.

Authors:  J P Shapleigh; J P Hosler; M M Tecklenburg; Y Kim; G T Babcock; R B Gennis; S Ferguson-Miller
Journal:  Proc Natl Acad Sci U S A       Date:  1992-06-01       Impact factor: 11.205

10.  Reaction of dioxygen with cytochrome c oxidase reduced to different degrees: indications of a transient dioxygen complex with copper-B.

Authors:  M Oliveberg; B G Malmström
Journal:  Biochemistry       Date:  1992-04-14       Impact factor: 3.162

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  14 in total

Review 1.  Pathways of proton transfer in cytochrome c oxidase.

Authors:  P Brzezinski; P Adelroth
Journal:  J Bioenerg Biomembr       Date:  1998-02       Impact factor: 2.945

2.  Kinetic coupling between electron and proton transfer in cytochrome c oxidase: simultaneous measurements of conductance and absorbance changes.

Authors:  P Adelroth; H Sigurdson; S Hallén; P Brzezinski
Journal:  Proc Natl Acad Sci U S A       Date:  1996-10-29       Impact factor: 11.205

Review 3.  Structure and evolution of cytochrome oxidase.

Authors:  M Saraste
Journal:  Antonie Van Leeuwenhoek       Date:  1994       Impact factor: 2.271

Review 4.  The superfamily of heme-copper respiratory oxidases.

Authors:  J A García-Horsman; B Barquera; J Rumbley; J Ma; R B Gennis
Journal:  J Bacteriol       Date:  1994-09       Impact factor: 3.490

Review 5.  Human cytochrome c oxidase: structure, function, and deficiency.

Authors:  J W Taanman
Journal:  J Bioenerg Biomembr       Date:  1997-04       Impact factor: 2.945

6.  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.

Authors:  M Santana; M M Pereira; N P Elias; C M Soares; M Teixeira
Journal:  J Bacteriol       Date:  2001-01       Impact factor: 3.490

7.  Design, synthesis, and characterization of a novel hemoprotein.

Authors:  Z Xu; R S Farid
Journal:  Protein Sci       Date:  2001-02       Impact factor: 6.725

8.  Femtosecond resolution of ligand-heme interactions in the high-affinity quinol oxidase bd: A di-heme active site?

Authors:  M H Vos; V B Borisov; U Liebl; J L Martin; A A Konstantinov
Journal:  Proc Natl Acad Sci U S A       Date:  2000-02-15       Impact factor: 11.205

9.  CuA and CuZ are variants of the electron transfer center in nitrous oxide reductase.

Authors:  J A Farrar; W G Zumft; A J Thomson
Journal:  Proc Natl Acad Sci U S A       Date:  1998-08-18       Impact factor: 11.205

Review 10.  Molecular genetics of the genus Paracoccus: metabolically versatile bacteria with bioenergetic flexibility.

Authors:  S C Baker; S J Ferguson; B Ludwig; M D Page; O M Richter; R J van Spanning
Journal:  Microbiol Mol Biol Rev       Date:  1998-12       Impact factor: 11.056

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