Distribution of valence electrons of the flavin cofactor in NADH-cytochrome b₅ reductase.

ABSTRACT: Flavin compounds such as flavin adenine dinucleotide (FAD), flavin mononucleotide and riboflavin make up the active centers in flavoproteins that facilitate various oxidoreductive processes. The fine structural features of the hydrogens and valence electrons of the flavin molecules in the protein environment are critical to the functions of the flavoproteins. However, information on these features cannot be obtained from conventional protein X-ray analyses at ordinary resolution. Here we report the charge density analysis of a flavoenzyme, NADH-cytochrome b₅ reductase (b5R), at an ultra-high resolution of 0.78 Å. Valence electrons on the FAD cofactor as well as the peptide portion, which are clearly visualized even after the conventional refinement, are analyzed by the multipola

SUBMITTER: Takaba K 

PROVIDER: S-EPMC5320556 | biostudies-literature | 2017 Feb

REPOSITORIES: biostudies-literature