Source:http://linkedlifedata.com/resource/pubmed/id/14674751
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
50
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pubmed:dateCreated |
2003-12-16
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pubmed:abstractText |
The interaction between bovine cytochrome b(5) (cyt b(5)) and horse heart cytochrome c (cyt c) is investigated by NMR spectroscopy. Chemical shifts of cyt b(5) backbone resonances and side chain methyl resonances were monitored as a function of cyt c concentration. The shifts are small but saturatable and indicate that the binding of cyt b(5) with cyt c is in fast exchange. An equilibrium association constant of (6 +/- 3) x 10(4) M(-1) was obtained with a lower limit of 180 s(-1) for the dissociation rate of the complex. To resolve considerable ambiguities in the interpretation of the chemical shift mapping, (15)N relaxation experiments and cross-saturation experiments were used as alternative methods to map the cyt b(5)-cyt c binding interface. Results from the three experiments combined demonstrate that the conserved negatively charged region of cyt b(5) surrounding the solvent-exposed heme edge is involved in the interaction with cyt c. These data support the models proposed by Salemme and Mauk [(1976) J. Mol. Biol. 102, 563-568; (1993) Biochemistry 32, 6613-6623].
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0006-2960
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
23
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pubmed:volume |
42
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
14774-84
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:14674751-Animals,
pubmed-meshheading:14674751-Binding Sites,
pubmed-meshheading:14674751-Carbon Isotopes,
pubmed-meshheading:14674751-Cattle,
pubmed-meshheading:14674751-Conserved Sequence,
pubmed-meshheading:14674751-Cytochromes b5,
pubmed-meshheading:14674751-Cytochromes c,
pubmed-meshheading:14674751-Horses,
pubmed-meshheading:14674751-Models, Chemical,
pubmed-meshheading:14674751-Models, Molecular,
pubmed-meshheading:14674751-Nitrogen Isotopes,
pubmed-meshheading:14674751-Nuclear Magnetic Resonance, Biomolecular,
pubmed-meshheading:14674751-Peptide Mapping,
pubmed-meshheading:14674751-Protein Binding,
pubmed-meshheading:14674751-Protein Conformation,
pubmed-meshheading:14674751-Surface Properties,
pubmed-meshheading:14674751-Thermodynamics
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pubmed:year |
2003
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pubmed:articleTitle |
Mapping the binding interface of the cytochrome b5-cytochrome c complex by nuclear magnetic resonance.
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pubmed:affiliation |
Department of Anesthesiology, University of Michigan, VA Medical Center, 2215 Fuller Road, Ann Arbor, Michigan 48105, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.
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