Premium
Distal Cu Ion Protects Synthetic Heme/Cu Analogues of Cytochrome Oxidase against Inhibition by CO and Cyanide
Author(s) -
Collman James P.,
Boulatov Roman,
Shiryaeva Irina M.,
Sunderland Christopher J.
Publication year - 2002
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/1521-3773(20021104)41:21<4139::aid-anie4139>3.0.co;2-p
Subject(s) - cyanide , chemistry , heme , oxidase test , cytochrome c oxidase , cyclic voltammetry , ion , heme a , combinatorial chemistry , stereochemistry , inorganic chemistry , enzyme , electrode , biochemistry , organic chemistry , electrochemistry
Iron loses its inhibitions! Comparative voltammetry of close functional heme/Cu B analogues (see picture) in the FeCu and Cu‐free forms revealed a Cu‐induced destabilization of CO and CN − ion binding to the Fe center. During steady‐state reduction of O 2 under physiologically relevant conditions, an up to fivefold higher concentration of CN − ion is required to inhibit the same fraction of the FeCu catalyst as of the Cu‐free analogues.