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 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.
Yamamoto
Yasuhiko
Y
Department of Chemistry, University of Tsukuba, Tsukuba 305-8571, Japan. yamamoto@staff.chem.tsukuba.ac.jp
Terui
Norifumi
N
Tachiiri
Naoki
N
Minakawa
Kazuhisa
K
Matsuo
Hitomi
H
Kameda
Tsunenori
T
Hasegawa
Jun
J
Sambongi
Yoshihiro
Y
Uchiyama
Susumu
S
Kobayashi
Yuji
Y
Igarashi
Yasuo
Y
D001426:Bacterial Proteins / Q000737:chemistry*; D001665:Binding Sites; D003574:Cytochrome c Group / Q000737:chemistry*; D006091:Gram-Negative Chemolithotrophic Bacteria / Q000737:chemistry; D006418:Heme / Q000737:chemistry; D006358:Hot Temperature; D007501:Iron / Q000737:chemistry*; D008715:Methionine / Q000737:chemistry*; D019906:Nuclear Magnetic Resonance, Biomolecular; D011487:Protein Conformation; D011550:Pseudomonas aeruginosa / Q000737:chemistry
D001426:Bacterial Proteins; D003574:Cytochrome c Group; D006418:Heme; D008715:Methionine; D007501:Iron