Cfrench:hemtoppage

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*Wilkins, R.G. 1992. Binuclear iron centres in proteins. ''Chemical Society Reviews'' '''?''', 171-178.
*Wilkins, R.G. 1992. Binuclear iron centres in proteins. ''Chemical Society Reviews'' '''?''', 171-178.
*Vanin, S., Negrisolo, E., Bailly, X., Bubacco, L., Beltramini, M., and Salvato, B. 2006. Molecular evolution and phylogeny of sipunculan hemerythrins. ''Journal of Molecular Evolution'' '''62'''. 32-41.
*Vanin, S., Negrisolo, E., Bailly, X., Bubacco, L., Beltramini, M., and Salvato, B. 2006. Molecular evolution and phylogeny of sipunculan hemerythrins. ''Journal of Molecular Evolution'' '''62'''. 32-41.
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{|
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|-
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!Organism!!Class!!Protein!!Accession
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|-
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|''Golfingia vulgaris''||Sipunculid||Octomeric hemerythrin||57282926 (chain 1), 57282928 (chain 2), 57282930 (chain 3), 57282932 (chain 4)
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|-
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|''Phascolopsis gouldii''||Sipunculid||Octomeric hemerythrin||21264441, 13787000 to 13787015
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|-
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|''Phascolopsis gouldii''||Sipunculid||Myohemerythrin||232242, 253340
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|-
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|''Themiste dyscritum''||Sipunculid||Octomeric hemerythrin||123041
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|-
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|''Themiste zostericola''||Sipunculid||Octomeric hemerythrin||123042, 3892004
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|-
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|''Themiste zostericola''||Sipunculid||Myohemerythrin||417114, 230634, 3892012
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|-
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|''Sipunculus nudus''||Sipunculid||Hemerythrin, 4˚ structure unclear: trimeric?||57282893 (chain A), 57282922 (chain B)
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|-
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|''Sipunculus nudus''||Sipunculid||Myohemerythrin||57282924
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|-
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|''Siphonosoma cumanense''||Sipunculid||Trimeric hemerythrin||123040
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|-
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|''Nereis diversicolor''||Polychaete (Annelid)||Myohemerythrin/ cadmium-binding protein MPTII||123030, 299077, 417311, 542500
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|-
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|''Perriserrula leucophryna''||Polychaete (Annelid)||Myohemerythrin||34327785
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|-
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|''Hirudo medicinalis''||Leech (Annelid)||Myohemerythrin (neurohemeythrin)||44921619
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|-
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|''Theromyzon tessulatum''||Leech (Annelid)||Myohemerythrin (ovohemerythrin?)||9887226, 21263690
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|-
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|''Lingula unguis''||Brachiopod||Octomeric hemerythrin, α4β4||243463, 123038 (chain α), 123044 (chain β)
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|-
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|''Lingula reevii''||Brachiopod||Octomeric hemerythrin, α4β4||833931, 46397821, 1091863 (chain α), 833932, 46397822, 1091864 (chain β)
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|-
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|''Naegleria fowleri''||Amoeba||Myohemerythrin-like protein NfaI||21263696, 7025498, 50983087
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|}
===What are bacteriohemerythrins?===
===What are bacteriohemerythrins?===
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[[Cfrench:hemlist1|List of prokaryote genera with putative bacteriohemerythrins]]
[[Cfrench:hemlist1|List of prokaryote genera with putative bacteriohemerythrins]]
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[[Cfrench:hemanalysis1|Analysis of short chain bacteriohemerythrins]]
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[[Cfrench:multidomhem|Analysis of multi-domain bacteriohemerythrins]]
[[Cfrench:labtoppage|French lab main page]]
[[Cfrench:labtoppage|French lab main page]]

Current revision

Contents

Hemerythrins

What are hemerythrins?

Hemerythrins are oxygen binding proteins found in certain invertebrates: sipunculid worms (peanut worms), brachiopods (lamp shells) and some annelid worms. One has also been found in an amoeba. They serve the same function as hemoglobin and myoglobin in vertebrates, but do not contain a heme prosthetic group; instead they contain non-heme iron. Each hemerythin subunit contains two iron atoms bound to a characteristic set of ligands - five histidines, one aspartate and one glutamate.

  • Stenkamp, R.E. 1994. Dioxygen and hemerythin. Chemical Reviews 94, 715-726.
  • Wilkins, R.G. 1992. Binuclear iron centres in proteins. Chemical Society Reviews ?, 171-178.
  • Vanin, S., Negrisolo, E., Bailly, X., Bubacco, L., Beltramini, M., and Salvato, B. 2006. Molecular evolution and phylogeny of sipunculan hemerythrins. Journal of Molecular Evolution 62. 32-41.
OrganismClassProteinAccession
Golfingia vulgarisSipunculidOctomeric hemerythrin57282926 (chain 1), 57282928 (chain 2), 57282930 (chain 3), 57282932 (chain 4)
Phascolopsis gouldiiSipunculidOctomeric hemerythrin21264441, 13787000 to 13787015
Phascolopsis gouldiiSipunculidMyohemerythrin232242, 253340
Themiste dyscritumSipunculidOctomeric hemerythrin123041
Themiste zostericolaSipunculidOctomeric hemerythrin123042, 3892004
Themiste zostericolaSipunculidMyohemerythrin417114, 230634, 3892012
Sipunculus nudusSipunculidHemerythrin, 4˚ structure unclear: trimeric?57282893 (chain A), 57282922 (chain B)
Sipunculus nudusSipunculidMyohemerythrin57282924
Siphonosoma cumanenseSipunculidTrimeric hemerythrin123040
Nereis diversicolorPolychaete (Annelid)Myohemerythrin/ cadmium-binding protein MPTII123030, 299077, 417311, 542500
Perriserrula leucophrynaPolychaete (Annelid)Myohemerythrin34327785
Hirudo medicinalisLeech (Annelid)Myohemerythrin (neurohemeythrin)44921619
Theromyzon tessulatumLeech (Annelid)Myohemerythrin (ovohemerythrin?)9887226, 21263690
Lingula unguisBrachiopodOctomeric hemerythrin, α4β4243463, 123038 (chain α), 123044 (chain β)
Lingula reeviiBrachiopodOctomeric hemerythrin, α4β4833931, 46397821, 1091863 (chain α), 833932, 46397822, 1091864 (chain β)
Naegleria fowleriAmoebaMyohemerythrin-like protein NfaI21263696, 7025498, 50983087

What are bacteriohemerythrins?

Recently, proteins with similar sequence to hemerythrins have been found in some bacteria. Two of these, from Methylococcus capsulatus and Desulfovibrio vulgaris, have been expressed in Escherichia coli, purified, and shown to possess iron atoms and to bind oxygen in the same way as animal hemerythrins. Searches of genomic sequence databases have shown that hemerythrin-like proteins (for which we propose the name 'bacteriohemerythrins') are present in many genera of bacteria. Some are simple single-domain hemerythrins like those of animals; in other cases the hemerythrin domain is fused to another domain, most commonly a signal transduction domain such as a methyl-accepting chemotaxis receptor (MCP), a GGDEF domain, or a histidine kinase domain. In these cases the hemerythrin presumably functions as an oxygen-sensing domain.

  • Xiong, J., Kurtz, D.M., Ai, J., and Sanders-Loehr, J. 2000. A hemerythrin-like domain in a bacterial chemotaxis protein. Biochemistry 39, 5117-5125.
  • Kao, W.-C., Chen, Y.-R., Yi, E.C., Lee, H., Tian, Q., Wu, K.-M., Tsai, S.-F., Yu, S.S.-F., Chen, Y.-J., Aebersold, R., and Chan, S.I. 2004. Quantitative proteomic analysis of metabolic regulation by copper ions in Methylococcus capsulatus (Bath). Journal of Biological Chemistry 279, 51554-51560.
  • Karlsen, O.A., Ramsevik, L., Bruseth, L.J., Larsen, O., Brenner, A., Berven, F.S., Jensen, H.B., and Lillehaug, J.R. 2005. Characterization of a prokaryotic hemerythrin from the methanotrophic bacterium Methylococcus capsulatus (Bath). FEBS Journal 272, 2428-2440.
  • Isaza, C.E., Silaghi-Dumitrescu, R., Iyer, R.B., Kurtz, D.M., and Chan, M.K. 2006. Structural Basis for O2 sensing by the hemerythrin-like domain of a bacterial chemotaxis protein: substrate tunnel and fluxional N-terminus. Biochemistry 45, 9023-9031.

Why are we interested in hemerythrins?

Mainly because we are interested in magnetotactic bacteria, and our sequence searches show that magnetotactic bacteria contain far more different bacteriohemerythrins than any other type of bacteria for which genome data are available. Most species with bacteriohemerythrins have only one or two; a few have five or six, a couple as many as ten. The two species of Magnetospirillum which have been sequenced appear to contain around thirty different bacteriohemerythrin genes each, and Magnetococcus at least seventeen. Surely they must be playing some important role in the magnetotactic lifestyle. Some of them, such as those with MCP domains, are probably involved in finding the zone with the low oxygen concentration required for good growth and magnetosome formation; others may be involved in oxygen storage or magnetite synthesis.

List of prokaryote genera with putative bacteriohemerythrins

Analysis of short chain bacteriohemerythrins

Analysis of multi-domain bacteriohemerythrins

French lab main page

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