Article
Glutamate 350 Plays an Essential Role in Conformational Gating of Long-Range Radical Transport in Escherichia coli Class Ia Ribonucleotide Reductase.
Biochemistry - 14 Feb 2017
Ravichandran Kanchana, Minnihan Ellen C, Lin Qinghui, Yokoyama Kenichi, Taguchi Alexander T, Shao Jimin, Nocera Daniel G, Stubbe JoAnne
Abstract excerpt
Escherichia coli class Ia ribonucleotide reductase (RNR) is composed of two subunits that form an active α2β2 complex. The nucleoside diphosphate substrates (NDP) are reduced in α2, 35 Å from the essential diferric-tyrosyl radical (Y122•) cofactor in β2. The Y122•-mediated oxidation of C439 in α2 occurs by a pathway (Y122 ⇆ [W48] ⇆ Y356 in β2 to Y731 ⇆ Y730 ⇆ C439 in α2) across the α/β interface. The absence of...
Topics
- Adenosine Triphosphate
- Amino Acid Substitution
- Apoenzymes
- Binding, Competitive
- Biocatalysis
- Cytidine Diphosphate
- Electron Spin Resonance Spectroscopy
- Electron Transport
- Escherichia coli Proteins
