Leonid A. Sazanov is a professor of structural biology at the Institute of Science and Technology Austria, Klosterneuburg. He graduated in biophysics from the Belarusian State University, Minsk, Belarus, and obtained his Ph.D. in biophysics from the Moscow State University in Russia. He moved to the United Kingdom in 1992 and worked at the University of Birmingham, Imperial College London and the Medical Research Council Laboratory of Molecular Biology (MRC LMB) in Cambridge. From 2000 until 2015 he led an independent research group in the MRC Mitochondrial Biology Unit in Cambridge. His research interests include mitochondrial and bacterial bioenergetics, as well as the structure and function of large membrane protein assemblies, in particular respiratory complex I. His studies have led to the determination of the first atomic structures of the two main domains and, recently, of the entire respiratory complex I, one of the largest membrane proteins solved so far. Leonid A. Sazanov's homepage
A process that links the electron transport chain to ATP synthesis.
Midpoint redox potential
(Em). A measure of the tendency of a chemical species to acquire electrons and thereby be reduced. The species with large positive potential have high affinity for electrons and vice versa. Em denotes the potential at which the compound is half oxidized and half reduced.
A class of redox cofactors found in molybdenum- and tungsten-containing enzymes, such as nitrate reductase.
The class of hydrogenases with the most members. [NiFe] hydrogenases catalyse the reversible 2H+ + 2e− ↔ H2 reaction; their core comprises the large subunit hosting the Ni–Fe active site and the small subunit hosting the Fe–S clusters.
(Also known as π–helix). A protein feature created by the insertion of a single additional amino acid into a pre-existing α-helix, destabilizing secondary structure in potential functional sites.
A proton-hopping mechanism, whereby protons travel through networks of water molecules and protonatable side chains via the formation and cleavage of hydrogen bonds.