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Molecular aspects of the electron transfer system which participates in the oxidation of ferrous ion by Thiobacillus ferrooxidans.
The enzymes and redox proteins, which participate in the oxidation of ferrous ion by the acidophilic iron-oxiding bacterium Thiobacillus ferrooxidans, have been isolated and characterized. They are… Expand
Occurrence of peptidyl D-amino acids in soluble fractions of several eubacteria, archaea and eukaryotes.
- Y. Nagata, T. Fujiwara, K. Kawaguchi-Nagata, Y. Fukumori, T. Yamanaka
- Biology, Medicine
- Biochimica et biophysica acta
- 8 January 1998
The occurrence of peptidyl D-amino acids in the aqueous soluble fractions was investigated in various eubacteria, some archaea and some eukaryotes. The contents of the D-enantiomers of serine,… Expand
Cytochrome c (553, Chlorobium thiosulfatophilum) is a sulphide‐cytochrome c reductase
T h r e e k inds o f c-Wpe w m c h r o m e s , ¢y tochzome~ e-551 , c-553 a nd e.555 have been isolated f r o m the green zulFhur b a c t e r i u m , ,L~lorobh~na t]~oaTglfa~ophitum I1,2]. Recen*ly ,… Expand
Molecular cloning of the gene encoding Thiobacillus ferrooxidans Fe(II) oxidase. High homology of the gene product with HiPIP.
- T. Kusano, T. Takeshima, +5 authors T. Yamanaka
- Medicine, Biology
- The Journal of biological chemistry
- 5 June 1992
The amino-terminal sequence of Thiobacillus ferrooxidans Fe(II) oxidase (linked to cytochrome c552) was determined, and the iro gene that encodes this enzyme was cloned using degenerate… Expand
The oxidation mechanisms of thiosulphate and sulphide in Chlorobium thiosulphatophilum: roles of cytochrome c-551 and cytochrome c-553.
Abstract A thiosulphate-cytochrome c reductase was highly purified from Chlorobium thiosulphatophilum and its properties were studied. The enzyme catalyses reduction with Na 2 S 2 O 3 of c… Expand
Corrosion by bacteria of concrete in sewerage systems and inhibitory effects of formates on their growth.
Not only sulfur-oxidizing bacteria but also an acidophilic iron-oxidizing bacterium (or bacteria) were found in the corroded concrete from several sewerage systems in Japan. The surface pH of… Expand
Purification of cytochrome a1c1 from Nitrobacter agilis and characterization of nitrite oxidation system of the bacterium
Cytochrome a1c1 was highly purified from Nitrobacter agilis. The cytochrome contained heme a and heme c of equimolar amount, and its reduced form showed absorption peaks at 587, 550, 521, 434 and 416… Expand
The nitrite oxidizing system of Nitrobacter winogradskyi.
Cytochrome components which participate in the oxidation of nitrite in Nitrobacter winogradskyi have been highly purified and their properties studied in detail. Cytochrome a1c1 is an iron-sulphur… Expand
Fe(II)-oxidizing enzyme purified from Thiobacillus ferrooxidans
An Fe(II)-oxidizing enzyme was purified from Thiobacillus ferrooxidans to an electrophoretically homogeneous state. The enzyme showed absorption peaks at 282 and 382 nm and contained 18–20 atoms of… Expand
Purification and characterization of two membrane-bound c-type cytochromes from a facultative alkalophilic Bacillus.
The membrane fraction of the facultative alkalophilic bacterium, Bacillus YN-2000, was found to contain considerably larger amounts of two c-type cytochromes, cytochromes c-553 and c-552, when the… Expand