Open AccessStructure of Physarum polycephalum cytochrome b 5 reductase at 1.56 Å resolution
Author(s) -
Kim Sangwoo,
Suga Michihiro,
Minami Yoshiko,
Ogasahara Kyoko,
Ikegami Terumi,
Yubisui Toshitsugu,
Tsukihara Tomitake
Publication year - 2007
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309107010731
Subject(s) - physarum polycephalum , reductase , resolution (logic) , chemistry , cytochrome c , crystallography , stereochemistry , biochemistry , enzyme , mitochondrion , artificial intelligence , computer science
Physarum polycephalum cytochrome b 5 reductase catalyzes the reduction of cytochrome b 5 by NADH. The structure of P. polycephalum cytochrome b 5 reductase was determined at a resolution of 1.56 Å. The molecular structure was compared with that of human cytochrome b 5 reductase, which had previously been determined at 1.75 Å resolution [Bando et al. (2004), Acta Cryst. D 60 , 1929–1934]. The high‐resolution structure revealed conformational differences between the two enzymes in the adenosine moiety of the FAD, the lid region and the linker region. The structural properties of both proteins were inspected in terms of hydrogen bonding, ion pairs, accessible surface area and cavity volume. The differences in these structural properties between the two proteins were consistent with estimates of their thermostabilities obtained from differential scanning calorimetry data.