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Oxygen-carrying proteins: three solutions to a common problem.

D M Kurtz1

  • 1Department of Chemistry, University of Georgia, Athens 30602, USA.

Essays in Biochemistry
|March 24, 2000
PubMed
Summary

Nature utilizes three distinct metalloprotein active sites—hemoglobin (iron), hemerythrin (di-iron), and hemocyanin (dicopper)—for reversible oxygen binding, with revised understanding of CO discrimination. These sites control oxygen activation and cleavage.

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Area of Science:

  • Biochemistry and Biophysics
  • Bioinorganic Chemistry
  • Structural Biology

Background:

  • Transition-metal ions with unpaired d-electrons are crucial for overcoming oxygen's kinetic inertness and controlling its reduction potential.
  • Nature employs three distinct active site types for reversible oxygen binding: hemoglobin (Hb, haem iron), hemerythrin (Hr, non-haem di-iron), and hemocyanin (Hcy, dicopper).

Purpose of the Study:

  • To elucidate the structural and mechanistic principles underlying reversible oxygen binding in different metalloprotein active sites.
  • To revise the understanding of oxygen and carbon monoxide discrimination mechanisms in hemoglobin.
  • To compare oxygen activation and cleavage mechanisms across different metalloprotein families.

Main Methods:

  • High-resolution X-ray crystallography to determine the structures of oxygen-carrying proteins.

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  • Spectroscopic analysis to characterize the electronic and structural properties of active sites.
  • Mechanistic studies to investigate the elementary steps of oxygen binding and release.

    • Main Results:

    • Reversible O2 binding involves formal oxidative additions at Fe(II) in Hb, [Fe(II),Fe(II)] in Hr, and [Cu(I),Cu(I)] in Hcy.
    • The O-O bond is weakened but not cleaved upon binding across all three systems.
    • Revised understanding of Hb's CO/O2 discrimination, emphasizing binding pocket polarity and geometry over distal histidine sterics.
    • Hemerythrin involves proton and electron transfer; its O2 binding/release kinetics require further delineation.
    • Hemocyanin exhibits unusual side-on O2 binding, explaining its low O-O frequency and diamagnetism.

    Conclusions:

    • Nature has evolved diverse yet effective strategies for reversible oxygen binding using metalloprotein active sites.
    • Binding pocket environment plays a critical role in modulating oxygen affinity and selectivity.
    • Comparative studies of O2-carrying proteins and their enzyme counterparts will clarify factors governing the balance between O2 binding and O-O bond cleavage.