Octoheme tetrathionate reductase; tetrathionate ⇄ thiosulfate.
MKQLLFIALAGMALQAQAANPHKDVLKGPFTTGSEVTTQCLTCHEEQATDMMKTSHWTWE
LEQKLPDRTVVRGKKNSINNFCVAISSNEPRCTSCHAGYGWKDNTFDFKDKTKVDCLICH
DTTGTYVKDPAGAGEPMAKLDLAKIAQNVGAPVRDNCGSCHFYGGGGDAVKHGDLDSSMA
YPDKATDVHMDSDGNNFQCQNCHTTEKHQISGNAMGVSPGGIDHIGCENCHDSAPHSNKK
LNTHTATVACQTCHIPFFAKNEPTKMQWDWSTAGDDKPETVDQYGKHTYQKKKGNFVWEK
MVKPQYAWYNGTANAYMAGDKMDSNVVTKLTYPMGDINDAKAKIYPFKVHTGKQIYDKKL
NIFITPKTYGKGGYWSEFDWNLAAKLGMEANPTMLEKGIKYSGEYDFAATEMWWRINHMV
SPKEQALNCNDCHNKGTRLDWQALGYQGDPMKNKQGPKHKQ468
| PMID | Title & Author | Abstract | Year | |
| 0 | 12368813 | Genome sequence of the dissimilatory metal ion-reducing bacterium Shewanella oneidensis.John F Heidelberg 1 , Ian T Paulsen, Karen E Nelson, Eric J Gaidos, William C Nelson, Timothy D Read, Jonathan A Eisen, Rekha Seshadri, Naomi Ward, Barbara Methe, Rebecca A Clayton, Terry Meyer, Alexandre Tsapin, James Scott, Maureen Beanan, Lauren Brinkac, Sean Daugherty, Robert T DeBoy, Robert J Dodson, A Scott Durkin, Daniel H Haft, James F Kolonay, Ramana Madupu, Jeremy D Peterson, Lowell A Umayam, Owen White, Alex M Wolf, Jessica Vamathevan, Janice Weidman, Marjorie Impraim, Kathy Lee, Kristy Berry, Chris Lee, Jacob Mueller, Hoda Khouri, John Gill, Terry R Utterback, Lisa A McDonald, Tamara V Feldblyum, Hamilton O Smith, J Craig Venter, Kenneth H Nealson, Claire M Fraser | Shewanella oneidensis is an important model organism for bioremediation studies because of its diverse respiratory capabilities, conferred in part by multicomponent, branched electron transport systems. Here we report the sequencing of the S. oneidensis genome, which consists of a 4,969,803-base pair circular chromosome with 4,758 predicted protein-encoding open reading frames (CDS) and a 161,613-base pair plasmid with 173 CDSs. We identified the first Shewanella lambda-like phage, providing a potential tool for further genome engineering. Genome analysis revealed 39 c-type cytochromes, including 32 previously unidentified in S. oneidensis, and a novel periplasmic [Fe] hydrogenase, which are integral members of the electron transport system. This genome sequence represents a critical step in the elucidation of the pathways for reduction (and bioremediation) of pollutants such as uranium (U) and chromium (Cr), and offers a starting point for defining this organism's complex electron transport systems and metal ion-reducing capabilities. | 2002 |
| 1 | 15361860 | Octaheme tetrathionate reductase is a respiratory enzyme with novel heme ligation.Christopher G Mowat 1 , Emma Rothery, Caroline S Miles, Lisa McIver, Mary K Doherty, Katy Drewette, Paul Taylor, Malcolm D Walkinshaw, Stephen K Chapman, Graeme A Reid | We have isolated a soluble cytochrome from Shewanella oneidensis that contains eight covalently attached heme groups and determined its crystal structure. One of these hemes exhibits novel ligation of the iron atom by the epsilon-amino group of a lysine residue, despite its attachment via a typical CXXCH motif. This heme is most likely the active site for tetrathionate reduction, a reaction catalyzed efficiently by this enzyme. | 2004 |
| 2 | 17659281 | An octaheme c-type cytochrome from Shewanella oneidensis can reduce nitrite and hydroxylamine.Sally J Atkinson , Christopher G Mowat, Graeme A Reid, Stephen K Chapman | A c-type cytochrome from Shewanella oneidensis MR-1, containing eight hemes, has been previously designated as an octaheme tetrathionate reductase (OTR). The structure of OTR revealed that the active site contains an unusual lysine-ligated heme, despite the presence of a CXXCH motif in the sequence that would predict histidine ligation. This lysine ligation has been previously observed only in the pentaheme nitrite reductases, suggesting that OTR may have a possible role in nitrite reduction. We have now shown that OTR is an efficient nitrite and hydroxylamine reductase and that ammonium ion is the product. These results indicate that OTR may have a role in the biological nitrogen cycle. | 2007 |
Mowat, C.G., Rothery, E., Miles, C.S., McIver, L., Doherty, M.K., Drewette, K., et al. (2004) Octaheme tetrathionate reductase is a respiratory enzyme with novel heme ligation. Nat Struct Mol Biol 11: 1023–1024.