作者: Yasar Akdogan , Veerappan Anbazhagan , Dariush Hinderberger , Dirk Schneider , None
DOI: 10.1021/BI300489S
关键词:
摘要: Cytochrome b(559)' is a transmembrane protein formed by homodimerization of the 44-residue PsbF polypeptide and noncovalent binding heme cofactor. The can dimerize in absence presence heme. To monitor structural alterations associated with to apo-cytochrome, we analyzed apo- holo-cytochrome structure electron paramagnetic resonance spectroscopy. Spin labeling amino acids located close domain cytochrome revealed that unconstrained Heme restricts conformational dynamics domain, resulting structurally more constricted structure.