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pH-Dependence of The Maximal Velocity of Cytochrome c Oxidase: Relation to Proton Translocation and Respiratory Control

  • Linda C. Gregory
  • Shelagh Ferguson-Miller

Abstract

Cytochrome c oxidase is an enzyme of the mitochondrial respiratory chain that catalyzes the transfer of electrons from cytochrome c to oxygen and couples the redox events to proton translocation across the inner membrane, thereby contributing to the formation of an electrochemical proton gradient. The mammalian enzyme is composed of 12-13 nonidentical subunits (1, 2) and contains at least four metal prosthetic groups. This level of complexity has made it difficult to determine what structural features are directly involved in the proton transfer process, or in other aspects of oxidase function.

Keywords

Cytochrome Oxidase Respiratory Control Methylene Bisacrylamide Respiratory Control Ratio Beef Heart 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

Abbreviations

CCCP

Carbonyl cyanide m-chlorophenylhydrazone

DCCD

N, N’ -dicyclohexylcarbodiimide

EDTA

ethylenediaminetetraacetic acid

H+ / e-

ratio of protons translocated per electron transferred by cytochrome oxidase

Hepes

4-(2-hydroxyethyl)-1-piperazineethanesulfonic acid

MES

2(N-morpholino)ethanesulfonic acid

RCR

respiratory control ratio

SDS-PAGE

sodium dodecyl sulfate Polyacrylamide gel electrophoresis

TMPD

N,N,N’,N’ tetramethyl-p-phenylenediamine

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Copyright information

© Plenum Press, New York 1987

Authors and Affiliations

  • Linda C. Gregory
    • 1
  • Shelagh Ferguson-Miller
    • 1
  1. 1.Department of BiochemistryMichigan State UniversityEast LansingUSA

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