AbstractElectron transfer between the redox centres is essential for the function of the haem–copper oxidases. To date, the fastest rate of electron transfer between the haem groups has been determined to be ca. 3×105 s−1. Here, we show by optical spectroscopy that about one half of this electron transfer actually occurs at least three orders of magnitude faster, after photolysis of carbon monoxide from the half-reduced bovine heart enzyme. We ascribe this to the true haem–haem electron tunnelling rate between the haem groups
Cytochrome bd-I is one of the three proton motive force-generating quinol oxidases in the O2-depend...
AbstractTime-resolved spectroscopic studies in our laboratory of bovine heart cytochrome c oxidase d...
AbstractThe paper presents a survey of time-resolved studies of charge translocation by cytochrome c...
AbstractElectron transfer between the redox centres is essential for the function of the haem–copper...
AbstractEvidence is presented that single electron reduction is sufficient for rapid electron transf...
International audienceIn cytochrome c oxidase, reduction of molecular oxygen in the active site requ...
International audienceFast intraprotein electron transfer reactions associated with enzymatic cataly...
AbstractWe have investigated the kinetics of the single-turnover reaction of fully reduced solubilis...
Abstract We present novel experimental evidence that, starting with the oxidized enzyme, the interna...
International audienceBiological electron transfer (eT) between redox-active cofactors is thought to...
AbstractWe have examined the temperature dependence of the intramolecular electron transfer (ET) bet...
AbstractThe reaction with O2 of equimolar mixtures of cytochrome c and cytochrome c oxidase in high ...
AbstractThe PM→F transition of the catalytic cycle of cytochrome c oxidase from bovine heart was inv...
Cytochrome <i>c</i> oxidase (cco) catalyzes the oxygen reduction reaction in most aerobically respir...
AbstractThe resting as well as the 420 nm and 428 nm forms of cytochrome oxidase have been studied i...
Cytochrome bd-I is one of the three proton motive force-generating quinol oxidases in the O2-depend...
AbstractTime-resolved spectroscopic studies in our laboratory of bovine heart cytochrome c oxidase d...
AbstractThe paper presents a survey of time-resolved studies of charge translocation by cytochrome c...
AbstractElectron transfer between the redox centres is essential for the function of the haem–copper...
AbstractEvidence is presented that single electron reduction is sufficient for rapid electron transf...
International audienceIn cytochrome c oxidase, reduction of molecular oxygen in the active site requ...
International audienceFast intraprotein electron transfer reactions associated with enzymatic cataly...
AbstractWe have investigated the kinetics of the single-turnover reaction of fully reduced solubilis...
Abstract We present novel experimental evidence that, starting with the oxidized enzyme, the interna...
International audienceBiological electron transfer (eT) between redox-active cofactors is thought to...
AbstractWe have examined the temperature dependence of the intramolecular electron transfer (ET) bet...
AbstractThe reaction with O2 of equimolar mixtures of cytochrome c and cytochrome c oxidase in high ...
AbstractThe PM→F transition of the catalytic cycle of cytochrome c oxidase from bovine heart was inv...
Cytochrome <i>c</i> oxidase (cco) catalyzes the oxygen reduction reaction in most aerobically respir...
AbstractThe resting as well as the 420 nm and 428 nm forms of cytochrome oxidase have been studied i...
Cytochrome bd-I is one of the three proton motive force-generating quinol oxidases in the O2-depend...
AbstractTime-resolved spectroscopic studies in our laboratory of bovine heart cytochrome c oxidase d...
AbstractThe paper presents a survey of time-resolved studies of charge translocation by cytochrome c...