Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
15
pubmed:dateCreated
1998-8-20
pubmed:abstractText
The deep sea hydrothermal tube worm Riftia pachyptila possesses a multihemoglobin system with three different extracellular hemoglobins (Hbs; V1, V2, and C1): two dissolved in the vascular blood, V1 and V2, and one in the coelomic fluid, C1. V1 consists of four heme-containing chains and four linker chains. The globin chains making up V2 and C1 are, with one exception, common to V1. Remarkably these Hbs are able to bind oxygen and sulfide simultaneously and reversibly at two different sites. Two of the globin chains found in these three Riftia Hbs possess one free Cys residue and for at least one of the globins, the b-Cys75 is conserved among vestimentifera (Lamellibrachia sp.) and pogonophora (Oligobrachia mashikoi). By selectively blocking the free Cys with N-ethylmaleimide and using electrospray ionization mass spectrometry experiments, we show that these Cys residues are involved in sulfide binding by Riftia Hbs. Moreover, we also demonstrate that the larger V1 Hb can form persulfide groups on its linker chains, a mechanism that can account for the higher sulfide-binding potential of this Hb.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/9671793-13522731, http://linkedlifedata.com/resource/pubmed/commentcorrection/9671793-13691729, http://linkedlifedata.com/resource/pubmed/commentcorrection/9671793-14023808, http://linkedlifedata.com/resource/pubmed/commentcorrection/9671793-14086740, http://linkedlifedata.com/resource/pubmed/commentcorrection/9671793-2295645, http://linkedlifedata.com/resource/pubmed/commentcorrection/9671793-2310374, http://linkedlifedata.com/resource/pubmed/commentcorrection/9671793-5447431, http://linkedlifedata.com/resource/pubmed/commentcorrection/9671793-8343528, http://linkedlifedata.com/resource/pubmed/commentcorrection/9671793-8568863, http://linkedlifedata.com/resource/pubmed/commentcorrection/9671793-8621528, http://linkedlifedata.com/resource/pubmed/commentcorrection/9671793-8621529, http://linkedlifedata.com/resource/pubmed/commentcorrection/9671793-8814231, http://linkedlifedata.com/resource/pubmed/commentcorrection/9671793-889569, http://linkedlifedata.com/resource/pubmed/commentcorrection/9671793-9030725, http://linkedlifedata.com/resource/pubmed/commentcorrection/9671793-9305968, http://linkedlifedata.com/resource/pubmed/commentcorrection/9671793-9408952, http://linkedlifedata.com/resource/pubmed/commentcorrection/9671793-942051
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0027-8424
pubmed:author
pubmed:issnType
Print
pubmed:day
21
pubmed:volume
95
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
8997-9002
pubmed:dateRevised
2010-9-13
pubmed:meshHeading
pubmed:year
1998
pubmed:articleTitle
S-Sulfohemoglobin and disulfide exchange: the mechanisms of sulfide binding by Riftia pachyptila hemoglobins.
pubmed:affiliation
Department of Biological Sciences and Marine Science Institute, University of California, Santa Barbara, CA 93106, USA. zal@lifesci.lscf.ucsb.edu
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, Non-P.H.S., Research Support, Non-U.S. Gov't