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Studies on the Mechanism of Electron Bifurcation Catalyzed by Electron Transferring Flavoprotein (Etf) and Butyryl-CoA Dehydrogenase (Bcd) of Acidaminococcus fermentans*
Kinetic, structural, and spectral data revealed a detailed picture of the bifurcation process, which enables anaerobic bacteria and archaea to reduce the low-potential [4Fe-4S] clusters of ferredoxin, which increases the efficiency of the substrate level and electron transport phosphorylations.
Conformational heterogeneity in closed and open states of the KcsA potassium channel in lipid bicelles
- Dorothy M Kim, I. Dikiy, V. Upadhyay, D. J. Posson, D. Eliezer, C. Nimigean
- Biology, ChemistryThe Journal of general physiology
- 1 August 2016
KcsA is a potassium channel that is gated open and closed by changes in pH. Kim et al. find that at least two conformational states exist for both closed and open KcsA channels using solution NMR.
Structure and catalytic mechanism of N(5),N(10)-methenyl-tetrahydromethanopterin cyclohydrolase.
- V. Upadhyay, U. Demmer, E. Warkentin, J. Moll, S. Shima, U. Ermler
- 23 October 2012
Methenyltetrahydromethanopterin (methenyl-H(4)MPT(+)) cyclohydrolase (Mch) catalyzes the interconversion of methenyl-H(4)MPT(+) and formyl-H(4)MPT in the one-carbon energy metabolism of methanogenic,…
High-Resolution Cryoelectron Microscopy Structure of the Cyclic Nucleotide-Modulated Potassium Channel MloK1 in a Lipid Bilayer.
Molecular characterization of methanogenic N(5)-methyl-tetrahydromethanopterin: Coenzyme M methyltransferase.
High-resolution cryo-EM structure of the cyclic nucleotide-modulated potassium channel MloK1 in a lipid bilayer
The electron crystallography structure of the cAMP-bound potassium channel MloK1 (PCO-refined)
Electron transferring flavoprotein of Acidaminococcus fermentans: Towards a mechanism of flavin-based electron bifurcation
Structure of KcsA with L24C/R117C mutations