Binuclear centre structure of terminal protonmotive oxidases.

S Brown; AJ Moody; R Mitchell; PR Rich

doi:10.1016/0014-5793(93)81296-c

Binuclear centre structure of terminal protonmotive oxidases.

S Brown, AJ Moody, R Mitchell, PR Rich

School of Biological and Marine Sciences

Research output: Contribution to journal › Article › peer-review

Abstract

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 CuA and haem a. We suggest several potential lines of investigation.

Original language	English
Pages (from-to)	216-223
Number of pages	0
Journal	FEBS Lett
Volume	316
Issue number	3
DOIs	https://doi.org/10.1016/0014-5793(93)81296-c
Publication status	Published - 1 Feb 1993

Keywords

Amino Acid Sequence
Animals
Bacterial Proteins
Biophysical Phenomena
Biophysics
Catalysis
Cattle
Cytochrome b Group
Electron Transport
Electron Transport Complex IV
Fungal Proteins
Heme
Ion Channels
Molecular Sequence Data
Oxidation-Reduction
Protein Conformation
Protein Structure
Tertiary
Protons
Sequence Alignment

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10.1016/0014-5793(93)81296-c

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title = "Binuclear centre structure of terminal protonmotive oxidases.",

abstract = "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 CuA and haem a. We suggest several potential lines of investigation.",

keywords = "Amino Acid Sequence, Animals, Bacterial Proteins, Biophysical Phenomena, Biophysics, Catalysis, Cattle, Cytochrome b Group, Electron Transport, Electron Transport Complex IV, Fungal Proteins, Heme, Ion Channels, Molecular Sequence Data, Oxidation-Reduction, Protein Conformation, Protein Structure, Tertiary, Protons, Sequence Alignment",

author = "S Brown and AJ Moody and R Mitchell and PR Rich",

year = "1993",

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day = "1",

doi = "10.1016/0014-5793(93)81296-c",

language = "English",

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pages = "216--223",

journal = "FEBS Lett",

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TY - JOUR

T1 - Binuclear centre structure of terminal protonmotive oxidases.

AU - Brown, S

AU - Moody, AJ

AU - Mitchell, R

AU - Rich, PR

PY - 1993/2/1

Y1 - 1993/2/1

N2 - 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 CuA and haem a. We suggest several potential lines of investigation.

AB - 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 CuA and haem a. We suggest several potential lines of investigation.

KW - Amino Acid Sequence

KW - Animals

KW - Bacterial Proteins

KW - Biophysical Phenomena

KW - Biophysics

KW - Catalysis

KW - Cattle

KW - Cytochrome b Group

KW - Electron Transport

KW - Electron Transport Complex IV

KW - Fungal Proteins

KW - Heme

KW - Ion Channels

KW - Molecular Sequence Data

KW - Oxidation-Reduction

KW - Protein Conformation

KW - Protein Structure

KW - Tertiary

KW - Protons

KW - Sequence Alignment

U2 - 10.1016/0014-5793(93)81296-c

DO - 10.1016/0014-5793(93)81296-c

M3 - Article

SN - 0014-5793

VL - 316

SP - 216

EP - 223

JO - FEBS Lett

JF - FEBS Lett

IS - 3

ER -

Binuclear centre structure of terminal protonmotive oxidases.

Abstract

Keywords

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