Literature DB >> 17819908

Blood function in the hydrothermal vent vestimentiferan tube worm.

A J Arp, J J Childress.   

Abstract

Extracellular hemoglobin in the whole blood of Riftia pachyptila has a high oxygen affinity (P50 = 1.8 millimeters of mercury at 3 degrees C), a moderate decrease in oxygen affinity at higher temperatures (P50 = 2.7 millimeters of mercury at 14 degrees C), a small effect of carbon dioxide on oxygen affinity (Delta log P50/Delta pH =-0.12), and a high oxygen carrying capacity (up to 11 milliliters of oxygen per 100 milliliters of blood). These characteristics are compatible with the high oxygen demand of chemoautotrophic metabolism in the variable vent environment.

Entities:  

Year:  1981        PMID： 17819908     DOI： 10.1126/science.213.4505.342

Source DB:  PubMed          Journal:  Science        ISSN： 0036-8075            Impact factor:   47.728


  15 in total

1.  Structure of an extracellular giant hemoglobin of the gutless beard worm Oligobrachia mashikoi.

Authors:  Nobutaka Numoto; Taro Nakagawa; Akiko Kita; Yuichi Sasayama; Yoshihiro Fukumori; Kunio Miki
Journal:  Proc Natl Acad Sci U S A       Date:  2005-10-03       Impact factor: 11.205

2.  Bacterial communities associated with "Pompei worms" from the East Pacific rise hydrothermal vents: SEM, TEM observations.

Authors:  F Gaill; D Desbruyères; D Prieur
Journal:  Microb Ecol       Date:  1987-03       Impact factor: 4.552

3.  Sulfide binding is mediated by zinc ions discovered in the crystal structure of a hydrothermal vent tubeworm hemoglobin.

Authors:  Jason F Flores; Charles R Fisher; Susan L Carney; Brian N Green; John K Freytag; Stephen W Schaeffer; William E Royer
Journal:  Proc Natl Acad Sci U S A       Date:  2005-02-14       Impact factor: 11.205

4.  Cold-adapted features of arginine kinase from the deep-sea clam Calyptogena kaikoi.

Authors:  Tomohiko Suzuki; Kentaro Yamamoto; Hiroshi Tada; Kouji Uda
Journal:  Mar Biotechnol (NY)       Date:  2011-10-21       Impact factor: 3.619

5.  Evolution of Sulfur Binding by Hemoglobin in Siboglinidae (Annelida) with Special Reference to Bone-Eating Worms, Osedax.

Authors:  Damien S Waits; Scott R Santos; Daniel J Thornhill; Yuanning Li; Kenneth M Halanych
Journal:  J Mol Evol       Date:  2016-04-21       Impact factor: 2.395

6.  Primary structure of a constituent polypeptide chain (AIII) of the giant haemoglobin from the deep-sea tube worm Lamellibrachia. A possible H2S-binding site.

Authors:  T Suzuki; T Takagi; S Ohta
Journal:  Biochem J       Date:  1990-02-15       Impact factor: 3.857

7.  Life in the extreme environment at a hydrothermal vent: haemoglobin in a deep-sea copepod.

Authors:  A F Sell
Journal:  Proc Biol Sci       Date:  2000-11-22       Impact factor: 5.349

8.  N-terminal amino acid sequence of the deep-sea tube worm haemoglobin remarkably resembles that of annelid haemoglobin.

Authors:  T Suzuki; T Takagi; S Ohta
Journal:  Biochem J       Date:  1988-10-15       Impact factor: 3.857

9.  Protonephridial Excretory System in Vestimentifera (Siboglinidae, Annelida).

Authors:  N N Rimskaya-Korsakova; N P Karaseva; E N Temereva; V V Malakhov
Journal:  Dokl Biol Sci       Date:  2018-03-13

10.  Primary structure of a dimeric haemoglobin from the deep-sea cold-seep clam Calyptogena soyoae.

Authors:  T Suzuki; T Takagi; S Ohta
Journal:  Biochem J       Date:  1989-05-15       Impact factor: 3.857
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