Influence of Amino Acid Side Chain Packing on Fe−Methionine Coordination in Thermostable Cytochrome c

Paramagnetic NMR and optical studies of the oxidized forms of mesophile Pseudomonas aeruginosa cytochrome c 551 and its quintuple mutant (F7A/V13M/F34Y/E43Y/V78I), and thermophile Hydrogenobacter thermophilus cytochrome c 552 demonstrated that the amino acid side chain packings in the protein interi...

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Bibliographic Details
Published in:	Journal of the American Chemical Society Vol. 124; no. 39; pp. 11574 - 11575
Main Authors:	Yamamoto, Yasuhiko, Terui, Norifumi, Tachiiri, Naoki, Minakawa, Kazuhisa, Matsuo, Hitomi, Kameda, Tsunenori, Hasegawa, Jun, Sambongi, Yoshihiro, Uchiyama, Susumu, Kobayashi, Yuji, Igarashi, Yasuo
Format:	Journal Article
Language:	English
Published:	Washington, DC American Chemical Society 02-10-2002
Subjects:	Analytical, structural and metabolic biochemistry Bacterial Proteins - chemistry Binding Sites Biological and medical sciences Cytochrome c Group - chemistry Fundamental and applied biological sciences. Psychology General aspects, investigation methods Gram-Negative Chemolithotrophic Bacteria - chemistry Heme - chemistry Hot Temperature Iron - chemistry Methionine - chemistry Molecular biophysics Nuclear Magnetic Resonance, Biomolecular Protein Conformation Proteins Pseudomonas aeruginosa - chemistry Spectroscopy : techniques and spectras Analytical chemistry Cytochrome c Absorption spectrometry Biochemical analysis Side chain Coordination Aminoacid Methionine Thermostable Biochemistry Iron NMR spectrometry
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Summary:	Paramagnetic NMR and optical studies of the oxidized forms of mesophile Pseudomonas aeruginosa cytochrome c 551 and its quintuple mutant (F7A/V13M/F34Y/E43Y/V78I), and thermophile Hydrogenobacter thermophilus cytochrome c 552 demonstrated that the amino acid side chain packings in the protein interior influence the coordination bond between the heme iron and the axial methionine in the proteins. The strength of heme axial coordinations was found to correlate with the overall protein thermostability.
Bibliography:	ark:/67375/TPS-MRG8Z8PS-B istex:08E696499BC6EF4FFAB01CEA0B5A4508D1C70DBE ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23
ISSN:	0002-7863 1520-5126
DOI:	10.1021/ja025597s