Thermostability of manganese- and iron-superoxide dismutases from Escherichia coli is determined by the characteristic position of a glutamine residue.
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The first structure of a cold-adapted superoxide dismutase (SOD): biochemical and structural characterization of iron SOD fromAliivibrio salmonicidaSuperoxide dismutases and superoxide reductases.The crystal structure of an eukaryotic iron superoxide dismutase suggests intersubunit cooperation during catalysis.Improving the thermostability and stress tolerance of an archaeon hyperthermophilic superoxide dismutase by fusion with a unique N-terminal domain.Specificity and phenetic relationships of iron- and manganese-containing superoxide dismutases on the basis of structure and sequence comparisons.Biochemical characterization of psychrophilic Mn-superoxide dismutase from newly isolated Exiguobacterium sp. OS-77.A Single Mutation is Sufficient to Modify the Metal Selectivity and Specificity of a Eukaryotic Manganese Superoxide Dismutase to Encompass Iron.Identification of three Superoxide dismutase genes from a Geobacillus sp.
P2860
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P2860
Thermostability of manganese- and iron-superoxide dismutases from Escherichia coli is determined by the characteristic position of a glutamine residue.
description
2002 nî lūn-bûn
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name
Thermostability of manganese- ...... sition of a glutamine residue.
@en
Thermostability of manganese- ...... sition of a glutamine residue.
@nl
type
label
Thermostability of manganese- ...... sition of a glutamine residue.
@en
Thermostability of manganese- ...... sition of a glutamine residue.
@nl
prefLabel
Thermostability of manganese- ...... sition of a glutamine residue.
@en
Thermostability of manganese- ...... sition of a glutamine residue.
@nl
P2093
P2860
P1433
P1476
Thermostability of manganese- ...... sition of a glutamine residue.
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P2093
Gary J Hunter
Joe V Bannister
Thérèse Hunter
P2860
P304
P356
10.1046/J.1432-1033.2002.03200.X
P407
P577
2002-11-01T00:00:00Z