Health & Environmental Research Online (HERO)


Print Feedback Export to File
3797993 
Journal Article 
Characterization of the soluble hydrogenase from Desulfovibrio africanus 
Nivière, V; Forget, N; Gayda, JP; Hatchikian, EC 
1986 
Yes 
Biochemical and Biophysical Research Communications
ISSN: 0006-291X
EISSN: 1090-2104 
139 
2 
658-665 
English 
3021136 
The soluble hydrogenase from Desulfovibrio africanus has been isolated and characterized. The enzyme consists of two subunits of 65 kDa and 27 kDa. Its absorption spectrum is typical of an iron-sulfur protein. The protein contains 12 iron atoms, 10 labile sulfur atoms and 0.9 nickel atom per molecule. D. africanus hydrogenase is rapidly activated under reducing conditions and exhibits a specific activity of 570 mumoles H2 evolved/min/mg. The EPR spectrum of the oxidized enzyme shows no Ni(III) signals. Upon reduction under hydrogen, the protein sample exhibits signals due to nickel with g values at 2.21, 2.17 and 2.01 correlating with the active state of the enzyme. 
NAAQS
• ISA-PM (2019)
     In Scope
          ST PM Respiratory