Protein structural changes associated with active and inactive states of hydrogenase from Thiocapsa roseopersicina

Gabor Tigyi, Csaba Bagyinka, Kornél L. Kovács

Research output: Contribution to journalArticle

8 Citations (Scopus)

Abstract

Electrophoretic and isoelectrofocusing behavior of the hydrogenase from Thiocapsa roseopersicina under various conditions revealed remarkable properties of this enzyme: there are two active forms which differ in their molecular masses as well as in oxygen sensitivity; the apparent molecular masses of the active hydrogenase forms (90 and 49 kDa) differ considerably from those in the inactive state (64, 34, and 15 kDa); the active forms and some of the inactivated ones can be transformed into each other reversibly; urea can unfold the 64 and 34 kDa proteins but not the 49 kDa form at room temperature; the pI of these proteins are different in the presence of urea. The results suggest large rearrangements in the hydrogenase protein structure which are associated with the enzymatically active and inactive states. It is concluded that reversible formation of disulfide bonds cannot be the major cause for maintaining the enzyme conformation. Strong hydrophobic interactions are suggested to be primarily responsible for the structural stability and for the rearrangements.

Original languageEnglish (US)
Pages (from-to)69-74
Number of pages6
JournalBiochimie
Volume68
Issue number1
DOIs
StatePublished - Jan 1 1986
Externally publishedYes

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Thiocapsa roseopersicina
Hydrogenase
Molecular mass
Urea
Proteins
Enzymes
Hydrophobic and Hydrophilic Interactions
Disulfides
Conformations
Oxygen
Temperature

All Science Journal Classification (ASJC) codes

  • Biochemistry

Cite this

Protein structural changes associated with active and inactive states of hydrogenase from Thiocapsa roseopersicina. / Tigyi, Gabor; Bagyinka, Csaba; Kovács, Kornél L.

In: Biochimie, Vol. 68, No. 1, 01.01.1986, p. 69-74.

Research output: Contribution to journalArticle

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