Spectroscopic characterization of a novel multiheme c-type cytochrome widely implicated in bacterial electron transport

M D Roldán; H J Sears; M R Cheesman; S J Ferguson; A J Thomson; B C Berks; D J Richardson

doi:10.1074/jbc.273.44.28785

Spectroscopic characterization of a novel multiheme c-type cytochrome widely implicated in bacterial electron transport

M D Roldán, H J Sears, M R Cheesman, S J Ferguson, A J Thomson, B C Berks, D J Richardson

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Abstract

NapC is a member of a family of bacterial membrane-anchored tetra-heme c-type cytochromes that participate in a number of respiratory electron transport pathways. They are postulated to mediate electron transfer between membrane quinols/quinones and soluble periplasmic enzymes. The water-soluble heme domain of NapC has been expressed as a periplasmic protein. Mediated redox potentiometry and characterization by UV-visible, magnetic circular dichroism, and electron paramagnetic resonance spectroscopies demonstrates that soluble NapC contains four low spin hemes, each with bis-histidine axial ligation and with midpoint reduction potentials of -56, -181, -207, and -235 mV.

Original language	English
Pages (from-to)	28785-28790
Number of pages	6
Journal	Journal of Biological Chemistry
Volume	273
Issue number	44
DOIs	https://doi.org/10.1074/jbc.273.44.28785
Publication status	Published - 30 Oct 1998

Keywords

Amino Acid Sequence
Bacteria
Base Sequence
Cytochrome c Group
DNA Primers
Electron Transport
Molecular Sequence Data
Potentiometry
Sequence Homology, Amino Acid
Spectrum Analysis
Journal Article
Research Support, Non-U.S. Gov't

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title = "Spectroscopic characterization of a novel multiheme c-type cytochrome widely implicated in bacterial electron transport",

abstract = "NapC is a member of a family of bacterial membrane-anchored tetra-heme c-type cytochromes that participate in a number of respiratory electron transport pathways. They are postulated to mediate electron transfer between membrane quinols/quinones and soluble periplasmic enzymes. The water-soluble heme domain of NapC has been expressed as a periplasmic protein. Mediated redox potentiometry and characterization by UV-visible, magnetic circular dichroism, and electron paramagnetic resonance spectroscopies demonstrates that soluble NapC contains four low spin hemes, each with bis-histidine axial ligation and with midpoint reduction potentials of -56, -181, -207, and -235 mV.",

keywords = "Amino Acid Sequence, Bacteria, Base Sequence, Cytochrome c Group, DNA Primers, Electron Transport, Molecular Sequence Data, Potentiometry, Sequence Homology, Amino Acid, Spectrum Analysis, Journal Article, Research Support, Non-U.S. Gov't",

author = "Rold{\'a}n, {M D} and Sears, {H J} and Cheesman, {M R} and Ferguson, {S J} and Thomson, {A J} and Berks, {B C} and Richardson, {D J}",

year = "1998",

month = oct,

day = "30",

doi = "10.1074/jbc.273.44.28785",

language = "English",

volume = "273",

pages = "28785--28790",

journal = "Journal of Biological Chemistry",

issn = "0021-9258",

publisher = "American Society for Biochemistry and Molecular Biology",

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TY - JOUR

T1 - Spectroscopic characterization of a novel multiheme c-type cytochrome widely implicated in bacterial electron transport

AU - Roldán, M D

AU - Sears, H J

AU - Cheesman, M R

AU - Ferguson, S J

AU - Thomson, A J

AU - Berks, B C

AU - Richardson, D J

PY - 1998/10/30

Y1 - 1998/10/30

N2 - NapC is a member of a family of bacterial membrane-anchored tetra-heme c-type cytochromes that participate in a number of respiratory electron transport pathways. They are postulated to mediate electron transfer between membrane quinols/quinones and soluble periplasmic enzymes. The water-soluble heme domain of NapC has been expressed as a periplasmic protein. Mediated redox potentiometry and characterization by UV-visible, magnetic circular dichroism, and electron paramagnetic resonance spectroscopies demonstrates that soluble NapC contains four low spin hemes, each with bis-histidine axial ligation and with midpoint reduction potentials of -56, -181, -207, and -235 mV.

AB - NapC is a member of a family of bacterial membrane-anchored tetra-heme c-type cytochromes that participate in a number of respiratory electron transport pathways. They are postulated to mediate electron transfer between membrane quinols/quinones and soluble periplasmic enzymes. The water-soluble heme domain of NapC has been expressed as a periplasmic protein. Mediated redox potentiometry and characterization by UV-visible, magnetic circular dichroism, and electron paramagnetic resonance spectroscopies demonstrates that soluble NapC contains four low spin hemes, each with bis-histidine axial ligation and with midpoint reduction potentials of -56, -181, -207, and -235 mV.

KW - Amino Acid Sequence

KW - Bacteria

KW - Base Sequence

KW - Cytochrome c Group

KW - DNA Primers

KW - Electron Transport

KW - Molecular Sequence Data

KW - Potentiometry

KW - Sequence Homology, Amino Acid

KW - Spectrum Analysis

KW - Journal Article

KW - Research Support, Non-U.S. Gov't

U2 - 10.1074/jbc.273.44.28785

DO - 10.1074/jbc.273.44.28785

M3 - Article

C2 - 9786877

SN - 0021-9258

VL - 273

SP - 28785

EP - 28790

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

IS - 44

ER -

Spectroscopic characterization of a novel multiheme c-type cytochrome widely implicated in bacterial electron transport

Abstract

Keywords

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