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Binuclear centre structure of terminal protonmotive oxidases
Author(s) -
Brown Simon,
Moody A.John,
Mitchell Roy,
Rich Peter R.
Publication year - 1993
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(93)81296-c
Subject(s) - chemistry , mutant , electron transport chain , cytochrome c oxidase , electron transport complex iv , enzyme , stereochemistry , cytochrome , biochemistry , terminal (telecommunication) , biophysics , biology , gene , computer science , telecommunications
The recent proliferation of data obtained from mutant forms of cytochrome oxidase and analogous enzymes has necessitated a re‐examination of existing structural models. A new model is proposed, consistent with these data, which brings several protonatable residues (Y244, D298, D300, T309, T316, K319, T326) into the vicinity of the binuclear centre, suggestive of a proton‐transferring function. In addition, we also consider those residues which may participate in electron transport between Cu A and haem a . We suggest several potential lines of investigation.

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