Structural Aspects of Hemerythrin and Myohemerythrin

Klippenstein, Gerald L.

doi:10.1093/icb/20.1.39

Cited by 40 publications

(17 citation statements)

References 27 publications

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“…Hemerythrin is known to contain a substantial amount of iron (Klotz et al 1957), so that an iron-sulfide interaction seems likely. In contrast to hemoglobin, hemerythrin binds oxygen by changing its valence from Fe2+ to ~e~+ (Klotz et al 1957, Klippenstein 1980. Our preliminary studies on the coelomic fluid show that the black component is associated in the erythrocytes and has a molecular weight > 10 kDa, when we used a centrifugation procedure that excludes molecules of this size.…”

Section: Discussionmentioning

confidence: 97%

Sulfide detoxification and tolerance in Halicryptus spinulosus (Priapulida): a multiple strategy

Oeschger¹,

Vetter²

1992

Mar. Ecol. Prog. Ser.

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Section: Discussionmentioning

confidence: 97%

Sulfide detoxification and tolerance in Halicryptus spinulosus (Priapulida): a multiple strategy

Oeschger¹,

Vetter²

1992

Mar. Ecol. Prog. Ser.

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“…Although Hr-like proteins have also been reported in prokaryotes [24–26] oxygen binding Hrs have only been reported from marine invertebrates belonging to Annelida (which include sipunculids; [27]) Brachiopoda, Priapulida, Bryozoa, and a single species of both Cnidaria ( Nematostella vectensis ) and Arthropoda ( Calanus finmarchicus ) [9, 18, 28, 29]. Given this phylogenetic breadth of animals, whether all metazoan Hrs share a common origin is debated [28, 29].…”

Section: Introductionmentioning

confidence: 99%

Discovery and evolution of novel hemerythrin genes in annelid worms

et al. 2017

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BackgroundDespite extensive study on hemoglobins and hemocyanins, little is known about hemerythrin (Hr) evolutionary history. Four subgroups of Hrs have been documented, including: circulating Hr (cHr), myohemerythrin (myoHr), ovohemerythrin (ovoHr), and neurohemerythrin (nHr). Annelids have the greatest diversity of oxygen carrying proteins among animals and are the only phylum in which all Hr subgroups have been documented. To examine Hr diversity in annelids and to further understand evolution of Hrs, we employed approaches to survey annelid transcriptomes in silico.ResultsSequences of 214 putative Hr genes were identified from 44 annelid species in 40 different families and Bayesian inference revealed two major clades with strong statistical support. Notably, the topology of the Hr gene tree did not mirror the phylogeny of Annelida as presently understood, and we found evidence of extensive Hr gene duplication and loss in annelids. Gene tree topology supported monophyly of cHrs and a myoHr clade that included nHrs sequences, indicating these designations are functional rather than evolutionary.ConclusionsThe presence of several cHrs in early branching taxa suggests that a variety of Hrs were present in the common ancestor of extant annelids. Although our analysis was limited to expressed-coding regions, our findings demonstrate a greater diversity of Hrs among annelids than previously reported.Electronic supplementary materialThe online version of this article (doi:10.1186/s12862-017-0933-z) contains supplementary material, which is available to authorized users.

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“…A summary of such values for different hemerythrins can be found in reference 16. In general, the P 50 values are in the range of 1±15 mmHg with Hill n values near 1.…”

Section: Activity Testmentioning

confidence: 99%

Hemerythrin

Stenkamp¹

2004

Handbook of Metalloproteins

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Hemerythrin is a non‐heme iron protein that serves as an oxygen transfer or storage protein in several marine invertebrate phyla (sipunculids, brachiopods, priapulids and annelids). Each protein subunit (13 500 kD) binds two iron atoms by histidine, aspartic acid, and glutamic acid side‐chains. The protein carboxylates and a μ‐oxygen atom bridge the iron atoms in a prototypic FeOFe complex that has been extensively studied. One iron binds exogenous ligands including dioxygen and small anions. The protein functions by reversibly adding dioxygen to a deoxy form containing ferrous iron to produce an oxy form containing ferric iron and a peroxo anion.

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Structural Aspects of Hemerythrin and Myohemerythrin

Cited by 40 publications

References 27 publications

Sulfide detoxification and tolerance in Halicryptus spinulosus (Priapulida): a multiple strategy

Sulfide detoxification and tolerance in Halicryptus spinulosus (Priapulida): a multiple strategy

Discovery and evolution of novel hemerythrin genes in annelid worms

Hemerythrin

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