NDLI: Role of the Aromatic Ring of Tyr43 in Tetraheme Cytochrome c 3 from Desulfovibrio vulgaris Miyazaki F

Content Provider	PubMed Central
Author	Ozawa, Kiyoshi Takayama, Yuki Yasukawa, Fumiko Ohmura, Tomoaki Cusanovich, Michael A. Tomimoto, Yusuke Ogata, Hideaki Higuchi, Yoshiki Akutsu, Hideo
Copyright Year	2003
Abstract	Tyrosine 43 is positioned parallel to the fifth heme axial ligand, His34, of heme 1 in the tetraheme cytochrome c 3. The replacement of tyrosine with leucine increased the redox potential of heme 1 by 44 and 35 mV at the first and last reduction steps, respectively; its effects on the other hemes are small. In contrast, the Y43F mutation hardly changed the potentials. It shows that the aromatic ring at this position contributes to lowering the redox potential of heme 1 locally, although this cannot be the major contribution to the extremely low redox potentials of cytochrome c 3. Furthermore, temperature-dependent line-width broadening in partially reduced samples established that the aromatic ring at position 43 participates in the control of the kinetics of intramolecular electron transfer. The rate of reduction of Y43L cytochrome c 3 by 5-deazariboflavin semiquinone under partially reduced conditions was significantly different from that of the wild type in the last stage of the reduction, supporting the involvement of Tyr43 in regulation of reduction kinetics. The mutation of Y43L, however, did not induce a significant change in the crystal structure.
Related Links	http://dx.doi.org/10.1016/s0006-3495(03)74756-0
Ending Page	3374
Page Count	8
Starting Page	3367
File Format	PDF
ISSN	00063495
e-ISSN	15420086
Journal	Biophysical Journal
Issue Number	5
Volume Number	85
Language	English
Publisher	Biophysical Society
Publisher Date	2003-11-01
Access Restriction	Open
Rights Holder	Biophysical Society
Subject Keyword	Biophysics Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Biophysics

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