The disease-associated mutation of the mitochondrial thiol oxidase Erv1 impairs cofactor binding during its catalytic reaction

The disease-associated mutation of the mitochondrial thiol oxidase Erv1 impairs cofactor binding during its catalytic reaction

10.1042/BJ20140679

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Bibliographic Details
Main Authors:	Ceh-Pavia, E, Ang, S.K, Spiller, M.P, Lu, H
Other Authors:	BIOLOGICAL SCIENCES
Format:	Article
Published:	Portland Press 2020
Subjects:	cytochrome c dimer fungal enzyme histidine mutant protein oligomer tetramer thiol oxidase tryptophan coenzyme cytochrome reductase GFER protein, human protein binding Article autosomal recessive disorder catalysis circular dichroism denaturation enzyme activity essential for respiration and viability 1 gene fluorescence spectroscopy fungal gene fungal strain gel filtration chromatography gene mutation hydrogen bond light scattering melting point molecular weight multiangle laser light scattering myopathy nonhuman oligomerization oxidation reduction reaction oxidation reduction state oxygen consumption pH protein conformation protein quaternary structure protein tertiary structure protein unfolding proton transport respiratory chain site directed mutagenesis temperature dependence thermostability ultraviolet spectroscopy wild type yeast amino acid sequence amino acid substitution chemical structure chemistry enzyme active site genetics human metabolism missense mutation molecular genetics muscle disease sequence homology Amino Acid Sequence Amino Acid Substitution Catalysis Catalytic Domain Coenzymes Cytochrome Reductases Humans Models, Molecular Molecular Sequence Data Muscular Diseases Mutation, Missense Protein Binding Protein Structure, Tertiary Sequence Homology, Amino Acid
Online Access:	https://scholarbank.nus.edu.sg/handle/10635/183892
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Institution:	National University of Singapore

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https://scholarbank.nus.edu.sg/handle/10635/183892