1J0P

Three dimensional Structure of the Y43L mutant of Tetraheme Cytochrome c3 from Desulfovibrio vulgaris Miyazaki F

Summary for 1J0P

• Entry DOI: 10.2210/pdb1j0p/pdb
• Related: 1J0O 2CDV
• Descriptor: Cytochrome c3, SULFATE ION, PROTOPORPHYRIN IX CONTAINING FE, ... (5 entities in total)
• Functional Keywords: tetraheme cytochrome c3, high resolution x-ray structure, y43l mutant, electron transport
• Biological source: Desulfovibrio vulgaris
• Total number of polymer chains: 1
• Total formula weight: 15020.57

Authors

Ozawa, K.,Yasukawa, F.,Kumagai, J.,Ohmura, T.,Cusanvich, M.A.,Tomimoto, Y.,Ogata, H.,Higuchi, Y.,Akutsu, H. (deposition date: 2002-11-19, release date: 2003-11-19, Last modification date: 2024-11-20)

Primary citation

Ozawa, K.,Takayama, Y.,Yasukawa, F.,Ohmura, T.,Cusanovich, M.A.,Tomimoto, Y.,Ogata, H.,Higuchi, Y.,Akutsu, H.
Role of the aromatic ring of Tyr43 in tetraheme cytochrome c(3) from Desulfovibrio vulgaris Miyazaki F.
Biophys.J., 85:3367-3374, 2003

PubMed 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.

PubMed: 14581238
DOI: 10.1016/S0006-3495(03)74756-0

Experimental method

X-RAY DIFFRACTION (0.91 Å)