On the rate of proton exchange with solvent of the catalytic histidine in flavocytochromeb2(yeast L-lactate dehydrogenase)
Author:
Funder
CNRS
North Atlantic Treaty Organization Science Program
Publisher
Wiley
Subject
Molecular Biology,Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1002/pro.5560030114/fullpdf
Reference51 articles.
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2. High-level expression of fully active yeast flavocytochrome b2 in Escherichia coli;Black;Biochem J,1989
3. Flavocytochrome b2: Kinetic studies by absorbance and electron paramagnetic resonance spectroscopy of electron distribution among prosthetic groups;Capeilère-Blandin;Eur J Biochem,1975
4. Parameter estimating procedures for the Michaelis-Menten model: Reply to Tsang & Hsu;Cornish-Bowden;J Theor Biol,1991
5. Substitution of Tyr 254 with Phe at the active site of flavocytochrome b2: Consequences on catalysis of lactate dehydrogenation;Dubois;Biochemistry,1990
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2. Radiation induced modification of tryptophan and tyrosine residues in flavocytochrome b2 in dilute aqueous solution;Radiation Physics and Chemistry;2000-07
3. About the pKaof the active-site histidine in flavocytochrome b2(yeast L-lactate dehydrogenase);Protein Science;1998-07
4. L-lactate oxidase and L-lactate monooxygenase: Mechanistic variations on a common structural theme;Biochimie;1995-01
5. Mutation to glutamine of histidine 373, the catalytic base of flavocytochrome b2 (L-lactate dehydrogenase);Biochimie;1995-01
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