scispace - formally typeset
Journal ArticleDOI

Kinetic studies of sulfite: cytochrome C oxidoreductase, thiosulfate-oxiding enzyme, and adenosine-5'-phosphosulfate reductase from thiobacillus thioparus.

Ronald M. Lyric, +1 more
- 01 May 1970 - 
- Vol. 48, Iss: 5, pp 594-603
TLDR
Kinetic studies were carried out on three enzymes purified from Thiobacillus thioparus: sulfite: cytochrome c oxidoreductase, thiosulfate-oxidizing enzyme, and adenosine-5′-phosphosulfate reductase.
Abstract
Kinetic studies were carried out on three enzymes purified from Thiobacillus thioparus: sulfite: cytochrome c oxidoreductase, thiosulfate-oxidizing enzyme, and adenosine-5′-phosphosulfate reductase. From the initial velocity and product inhibition studies a tentative kinetic mechanism was proposed for each enzyme reaction.

read more

Citations
More filters
Journal ArticleDOI

Biochemistry of the chemolithotrophic oxidation of inorganic sulphur.

TL;DR: The relations between oxidation mechanisms, substrate-level and electron transport-dependent phosphorylation, energy-dependent NAD+ reduction and efficiency of growth are assessed in order to evaluate the efficiency of energy conservation in different species.
Journal ArticleDOI

Purification and properties of sulfite oxidase from chicken liver. Presence of molybdenum in sulfite oxidase from diverse sources.

TL;DR: Sulfite oxidase (EC 1.8.3.1) has been purified from chicken liver by modification of a procedure previously applied to bovine liver, suggesting an associating system whose state of association depends on both enzyme concentration and anion content.
Journal ArticleDOI

Cellular Location and' Partial Purification of the 'Thiosulphate-oxidizing Enzyme' and 'Trithionate Hydrolyase' from Thiobacillus tepidarius

Wei-Ping Lu, +1 more
- 01 Apr 1988 - 
TL;DR: The enzyme oxidizing thiosulphate to tetrathionate (‘tetrath ionate synthase’) has been purified and a scheme is presented which is consistent with all the whole organism and enzyme data available to date.
Journal ArticleDOI

A sulphite-dependent nitrate reductase from Thiobacillus denitrificans

TL;DR: A dissimilatory nitrate reductase from Thiobacillus denitrificans utilizes sulphite as an electron donor, with a pH optimum at 8.5.
Related Papers (5)