Evolution of the haem-haem interaction in vertebrate haemoglobins - a hypothesis

S. Vuk-Pavlović

Research output: Contribution to journalArticle

2 Citations (Scopus)

Abstract

A hypothesis about the evolution of the haem-haem interaction in haemoglobins has been formulated on the basis of available functional and structural data. It emerges that this cooperative mechanism is not necessarily due solely to the higher levels of protomer aggregation, because it occurs only in haemoglobins having the distal histidine. It is thus proposed that this amino acid residue might have had a significant role for the development of low-oxygen-affinity haemoglobins in vertebrates.

Original languageEnglish (US)
Pages (from-to)209-214
Number of pages6
JournalJournal of Molecular Evolution
Volume6
Issue number3
DOIs
StatePublished - Sep 1975
Externally publishedYes

Fingerprint

hemoglobin
Heme
Vertebrates
vertebrate
Hemoglobins
vertebrates
Protein Subunits
protein subunits
histidine
Histidine
cooperatives
Agglomeration
amino acid
Oxygen
oxygen
Amino Acids
amino acids

Keywords

  • Distal Histidine
  • Haem-Haem Interaction
  • Oxygen Affinity
  • Protomer Aggregation

ASJC Scopus subject areas

  • Genetics(clinical)
  • Molecular Biology
  • Genetics
  • Biochemistry
  • Biochemistry, Genetics and Molecular Biology(all)
  • Ecology, Evolution, Behavior and Systematics
  • Agricultural and Biological Sciences (miscellaneous)
  • Agricultural and Biological Sciences(all)

Cite this

Evolution of the haem-haem interaction in vertebrate haemoglobins - a hypothesis. / Vuk-Pavlović, S.

In: Journal of Molecular Evolution, Vol. 6, No. 3, 09.1975, p. 209-214.

Research output: Contribution to journalArticle

@article{b08490c30565418e8651c80212865dfc,
title = "Evolution of the haem-haem interaction in vertebrate haemoglobins - a hypothesis",
abstract = "A hypothesis about the evolution of the haem-haem interaction in haemoglobins has been formulated on the basis of available functional and structural data. It emerges that this cooperative mechanism is not necessarily due solely to the higher levels of protomer aggregation, because it occurs only in haemoglobins having the distal histidine. It is thus proposed that this amino acid residue might have had a significant role for the development of low-oxygen-affinity haemoglobins in vertebrates.",
keywords = "Distal Histidine, Haem-Haem Interaction, Oxygen Affinity, Protomer Aggregation",
author = "S. Vuk-Pavlović",
year = "1975",
month = "9",
doi = "10.1007/BF01732357",
language = "English (US)",
volume = "6",
pages = "209--214",
journal = "Journal of Molecular Evolution",
issn = "0022-2844",
publisher = "Springer New York",
number = "3",

}

TY - JOUR

T1 - Evolution of the haem-haem interaction in vertebrate haemoglobins - a hypothesis

AU - Vuk-Pavlović, S.

PY - 1975/9

Y1 - 1975/9

N2 - A hypothesis about the evolution of the haem-haem interaction in haemoglobins has been formulated on the basis of available functional and structural data. It emerges that this cooperative mechanism is not necessarily due solely to the higher levels of protomer aggregation, because it occurs only in haemoglobins having the distal histidine. It is thus proposed that this amino acid residue might have had a significant role for the development of low-oxygen-affinity haemoglobins in vertebrates.

AB - A hypothesis about the evolution of the haem-haem interaction in haemoglobins has been formulated on the basis of available functional and structural data. It emerges that this cooperative mechanism is not necessarily due solely to the higher levels of protomer aggregation, because it occurs only in haemoglobins having the distal histidine. It is thus proposed that this amino acid residue might have had a significant role for the development of low-oxygen-affinity haemoglobins in vertebrates.

KW - Distal Histidine

KW - Haem-Haem Interaction

KW - Oxygen Affinity

KW - Protomer Aggregation

UR - http://www.scopus.com/inward/record.url?scp=0016772559&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0016772559&partnerID=8YFLogxK

U2 - 10.1007/BF01732357

DO - 10.1007/BF01732357

M3 - Article

C2 - 1206726

AN - SCOPUS:0016772559

VL - 6

SP - 209

EP - 214

JO - Journal of Molecular Evolution

JF - Journal of Molecular Evolution

SN - 0022-2844

IS - 3

ER -