Journal article

THE HETERODISULFIDE REDUCTASE FROM METHANOBACTERIUM-THERMOAUTOTROPHICUM CONTAINS SEQUENCE MOTIFS CHARACTERISTIC OF PYRIDINE-NUCLEOTIDE-DEPENDENT THIOREDOXIN REDUCTASES


Authors listHEDDERICH, R; KOCH, J; LINDER, D; THAUER, RK

Publication year1994

Pages253-261

JournalEuropean Journal of Biochemistry

Volume number225

Issue number1

ISSN0014-2956

Open access statusBronze

DOI Linkhttps://doi.org/10.1111/j.1432-1033.1994.00253.x

PublisherWiley: No OnlineOpen


Abstract
The genes hdrA, hdrB and hdrC, encoding the three subunits of the iron-sulfur flavoprotein heterodisulfide reductase, have been cloned and sequenced. HdrA (72.19 kDa) was found to contain a region of amino acid sequence highly similar to the FAD-binding domain of pyridine-nucleotide-dependent disulfide oxidoreductases. Additionally, 110 amino acids C-terminal to the FAD-binding consensus, a short polypeptide stretch (VX(2)CATID) was detected which shows similarity to the region of thioredoxine reductase that contains the active-site cysteine residues (VX(2)CATCD). These findings suggest that HdrA harbors the site of heterodisulfide reduction and that the catalytic mechanism of the enzyme is similar to that of pyridine-nucleotide-dependent thioredoxin reductase. HdrA was additionally found to contain four copies of the sequence motif CX(2)CX(2)CX(3)C(P), indicating the presence of four [4Fe-4S] clusters. Two such sequence motifs were also present in HdrC (21.76 kDa), the N-terminal amino acid sequence of which showed sequence similarity to the gamma-subunit of the anaerobic glycerol-3-phosphate dehydrogenase of Escherichia coli. HdrC is therefore considered to be an electron carrier protein that contains two [4Fe-4S] clusters. HdrB (33.46 kDa) did not show sequence similarity to other known proteins, but appears to possess a C-terminal hydrophobic alpha-helix that might function as a membrane anchor. Although hdrB and hdrC are juxtaposed, these genes are not near hdrA.



Citation Styles

Harvard Citation styleHEDDERICH, R., KOCH, J., LINDER, D. and THAUER, R. (1994) THE HETERODISULFIDE REDUCTASE FROM METHANOBACTERIUM-THERMOAUTOTROPHICUM CONTAINS SEQUENCE MOTIFS CHARACTERISTIC OF PYRIDINE-NUCLEOTIDE-DEPENDENT THIOREDOXIN REDUCTASES, European Journal of Biochemistry, 225(1), pp. 253-261. https://doi.org/10.1111/j.1432-1033.1994.00253.x

APA Citation styleHEDDERICH, R., KOCH, J., LINDER, D., & THAUER, R. (1994). THE HETERODISULFIDE REDUCTASE FROM METHANOBACTERIUM-THERMOAUTOTROPHICUM CONTAINS SEQUENCE MOTIFS CHARACTERISTIC OF PYRIDINE-NUCLEOTIDE-DEPENDENT THIOREDOXIN REDUCTASES. European Journal of Biochemistry. 225(1), 253-261. https://doi.org/10.1111/j.1432-1033.1994.00253.x



Keywords


COENZYME-MFLAVOPROTEIN DISULFIDE OXIDOREDUCTASESSTRAIN MARBURG

Last updated on 2025-10-06 at 12:18