Molecular aspects of the electron transfer system which participates in the oxidation of ferrous ion by Thiobacillus ferrooxidans

Yamanaka, Tateo

doi:10.1016/0168-6445(95)00023-2

Cited by 31 publications

(53 citation statements)

References 34 publications

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“…Among the cytochromes C~~~( S ) (13 kDa), cSS2(m) (21 kDa), and csso(m) (68 kDa) described by Yamanaka [17], only ~~~~( s ) , which is not auto-oxizable, in contrast to cytochrome c, , seems to be involved in the respiratory chain. Cytochrome c,,,(s) is reduced by Fe(I1) : cytochrome c-oxidoreductase in the presence of Fez+ at pH 3.5 and is oxidised by cytochrome oxidase.…”

Section: Discussionmentioning

confidence: 98%

“…Surprisingly, upon aligning the two cytochromes isolated from two different strains of 7: ferrooxidans, they were found to have a large degree of identity (64%). The two cytochromes c552 (soluble and membrane bound) isolated by Yamanaka [17] …”

Section: Discussionmentioning

confidence: 99%

“…The cytochrome c , been purified, however, and its molecular mass was estiinated to be 22.3 kDa [16]. The N-terminal sequences of cytochromes c5?,(s) and c,,,(m) are nevertheless identical [17].…”

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confidence: 99%

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Characterisation of a Soluble Cytochrome c₄ Isolated from Thiobacillus ferrooxidans

Cavazza

Giudici‐Orticoni

Nitschke

et al. 1996

European Journal of Biochemistry

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A soluble c-type cytochrome was purified to homogeneity from Thiobacillus ferrooxidans. This cytochrome is characterised by an a-peak wavelength of 552 nm, a molecular mass of 21 193 Da (as determined by mass spectroscopy), and a PI value of 9. N-terminal sequencing yielded the polypeptide sequence up to the 50th residue. The iron content of 1.9 Fe/molecule and the heme/molecule ratio of 2.15 identified this cytochrome as a diheme protein. Optical redox titrations at pH 3.0 revealed the presence of two distinguishable redox species with E,,, = 385 mV 2 20 mV and Em = 480 mV 2 20 mV. EPR spectra recorded on this heme protein showed the presence of two distinct spectral species with g, = 3.1 and g, = 3.35. The g, = 3.35 heme corresponds to the higher potential redox species. In line with the differences in Em values, the two heme species were oxidised by 0, with significantly differing half-times.All the above mentioned properties demonstrate that this heme protein belongs to the c4 family of diheme cytochromes. The characteristics and functional role of the studied heme protein are discussed with reference to other c-type cytochromes described in Thiobacilli. Its properties are furthermore compared to other members of the cytochrome c4 family.

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Section: Discussionmentioning

confidence: 98%

Section: Discussionmentioning

confidence: 99%

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Characterisation of a Soluble Cytochrome c₄ Isolated from Thiobacillus ferrooxidans

Cavazza

Giudici‐Orticoni

Nitschke

et al. 1996

European Journal of Biochemistry

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“…The exact role of each of these carriers in the electron transport pathway of Fe(II) oxidation, however, is uncertain and controversial. In particular, there is debate on where Fe(II) oxidation takes place in the cell (2,5,58), although there is general agreement that the Fe(II) oxidase is located external to the cytoplasmic membrane.…”

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confidence: 99%

Isolation and Characterization of a Genetically Tractable Photoautotrophic Fe(II)-Oxidizing Bacterium, Rhodopseudomonas palustris Strain TIE-1

Jiao

Kappler

Croal

et al. 2005

Appl Environ Microbiol

199

209

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We report the isolation and characterization of a phototrophic ferrous iron [Fe(II)]-oxidizing bacterium named TIE-1 that differs from other Fe(II)-oxidizing phototrophs in that it is genetically tractable. Under anaerobic conditions, TIE-1 grows photoautotrophically with Fe(II), H 2 , or thiosulfate as the electron donor and photoheterotrophically with a variety of organic carbon sources. TIE-1 also grows chemoheterotrophically in the dark. This isolate appears to be a new strain of the purple nonsulfur bacterial species Rhodopseudomonas palustris, based on physiological and phylogenetic analysis. Fe(II) oxidation is optimal at pH 6.5 to 6.9. The mineral products of Fe(II) oxidation are pH dependent: below pH 7.0 goethite (␣-FeOOH) forms, and above pH 7.2 magnetite (Fe 3 O 4 ) forms. TIE-1 forms colonies on agar plates and is sensitive to a variety of antibiotics. A hyperactive mariner transposon is capable of random insertion into the chromosome with a transposition frequency of ϳ10 ؊5 . To identify components involved in phototrophic Fe(II) oxidation, mutants of TIE-1 were generated by transposon mutagenesis and screened for defects in Fe(II) oxidation in a cell suspension assay. Among approximately 12,000 mutants screened, 6 were identified that are specifically impaired in Fe(II) oxidation. Five of these mutants have independent disruptions in a gene that is predicted to encode an integral membrane protein that appears to be part of an ABC transport system; the sixth mutant has an insertion in a gene that is a homolog of CobS, an enzyme involved in cobalamin (vitamin B 12 ) biosynthesis.

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“…Although the same amounts of ferrous iron were oxidized when strains MON-1 and ATCC 23270 gave maximum cell yields, the growth yield of strain MON-1 was It is well known that aa 3 type cytochrome c oxidase is one of the most important components of the iron oxidation enzyme system in A. ferrooxidans. 32,[35][36][37][38][39][40][41][42][43][44] We have found that mercury resistant-A. ferrooxidans strains SUG 2-2 and MON-1 have high Fe 2þ -dependent mercury volatilization activity in the cells, 30,31) and that cytochrome c oxidase purified from strain SUG 2-2 reduces Hg 2þ with Fe 2þ as electron donor volatilizing metalic mercury (Hg 0 ) outside of the cells.…”

Section: Growth Of a Ferrooxidans Strains In An Iron Medium Supplemementioning

confidence: 99%

Reduction of Hg²⁺with Reduced Mammalian Cytochromecby CytochromecOxidase Purified from a Mercury-ResistantAcidithiobacillus ferrooxidansStrain, MON-1

Sugio

Fujii

Ninomiya

et al. 2008

Bioscience, Biotechnology, and Biochemistry

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Molecular aspects of the electron transfer system which participates in the oxidation of ferrous ion by Thiobacillus ferrooxidans

Cited by 31 publications

References 34 publications

Characterisation of a Soluble Cytochrome c₄ Isolated from Thiobacillus ferrooxidans

Characterisation of a Soluble Cytochrome c₄ Isolated from Thiobacillus ferrooxidans

Isolation and Characterization of a Genetically Tractable Photoautotrophic Fe(II)-Oxidizing Bacterium, Rhodopseudomonas palustris Strain TIE-1

Reduction of Hg²⁺with Reduced Mammalian Cytochromecby CytochromecOxidase Purified from a Mercury-ResistantAcidithiobacillus ferrooxidansStrain, MON-1

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Molecular aspects of the electron transfer system which participates in the oxidation of ferrous ion by Thiobacillus ferrooxidans

Cited by 31 publications

References 34 publications

Characterisation of a Soluble Cytochrome c4 Isolated from Thiobacillus ferrooxidans

Characterisation of a Soluble Cytochrome c4 Isolated from Thiobacillus ferrooxidans

Isolation and Characterization of a Genetically Tractable Photoautotrophic Fe(II)-Oxidizing Bacterium, Rhodopseudomonas palustris Strain TIE-1

Reduction of Hg2+with Reduced Mammalian Cytochromecby CytochromecOxidase Purified from a Mercury-ResistantAcidithiobacillus ferrooxidansStrain, MON-1

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Characterisation of a Soluble Cytochrome c₄ Isolated from Thiobacillus ferrooxidans

Characterisation of a Soluble Cytochrome c₄ Isolated from Thiobacillus ferrooxidans

Reduction of Hg²⁺with Reduced Mammalian Cytochromecby CytochromecOxidase Purified from a Mercury-ResistantAcidithiobacillus ferrooxidansStrain, MON-1