Open AccessEvidence for Distinct Electron Transfer Processes in Terminal Oxidases from Different Origin by Means of Protein Film Voltammetry
Author(s) -
Thomas Meyer,
Frédéric Melin,
Hao Xie,
Iris von der Hocht,
Sylvia K. Choi,
Mohamed R. Noor,
Hartmut Michel,
Robert B. Gennis,
Tewfik Soulimane,
Petra Hellwig
Publication year - 2014
Publication title -
journal of the american chemical society
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.115
H-Index - 612
eISSN - 1520-5126
pISSN - 0002-7863
DOI - 10.1021/ja505126v
Subject(s) - paracoccus denitrificans , thermus thermophilus , chemistry , electron transfer , cytochrome c oxidase , thermostability , multicopper oxidase , enzyme , cytochrome c , hemeprotein , cytochrome , electron transport complex iv , colloidal gold , electron transport chain , heme a , copper , rubredoxin , heme , biochemistry , nanoparticle , photochemistry , organic chemistry , chemical engineering , laccase , mitochondrion , escherichia coli , gene , engineering
Cytochrome aa3 from Paracoccus denitrificans and cytochrome ba3 from Thermus thermophilus, two distinct members of the heme-copper oxidase superfamily, were immobilized on electrodes modified with gold nanoparticles. This procedure allowed us to achieve direct electron transfer between the enzyme and the gold nanoparticles and to obtain evidence for different electrocatalytic properties of the two enzymes. The pH dependence and thermostability reveal that the enzymes are highly adapted to their native environments. These results suggest that evolution resulted in different solutions to the common problem of electron transfer to oxygen.
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