Display options
Cite
Ioannidis N, Cooper CE, Poole RK. Spectroscopic studies on an oxygen-binding haemoglobin-like flavohaemoprotein from Escherichia coli. Biochem J. 1992;288:649-55doi: 10.1042/bj2880649.
Ioannidis, N., Cooper, C. E., & Poole, R. K. (1992). Spectroscopic studies on an oxygen-binding haemoglobin-like flavohaemoprotein from Escherichia coli. The Biochemical journal, 288649-55. https://doi.org/10.1042/bj2880649
Ioannidis, N, et al. "Spectroscopic studies on an oxygen-binding haemoglobin-like flavohaemoprotein from Escherichia coli." The Biochemical journal vol. 288 (1992): 649-55. doi: https://doi.org/10.1042/bj2880649
Ioannidis N, Cooper CE, Poole RK. Spectroscopic studies on an oxygen-binding haemoglobin-like flavohaemoprotein from Escherichia coli. Biochem J. 1992 Dec 01;288:649-55. doi: 10.1042/bj2880649. PMID: 1334413; PMCID: PMC1132060.
Copy Download .nbib Format: NLM
Share it on
Full text links
Silverchair Information Systems Free PMC Article

Biochem J. 1992 Dec 01;288:649-55. doi: 10.1042/bj2880649.

Spectroscopic studies on an oxygen-binding haemoglobin-like flavohaemoprotein from Escherichia coli.

The Biochemical journal

N Ioannidis, C E Cooper, R K Poole

Affiliations

  1. Division of Biosphere Sciences, King's College, University of London, U.K.

PMID: 1334413 PMCID: PMC1132060 DOI: 10.1042/bj2880649
Free PMC Article

Abstract

The Escherichia coli haemoglobin-like flavohaemoprotein (Hmp) has been purified to near homogeneity using two chromatographic steps. The prosthetic groups are identified as FAD and protohaem IX. SDS/PAGE has indicated a molecular mass of 44 kDa for the monomeric protein consistent with the amino-acid sequence deduced from the hmp+ gene. The protein, as isolated, is in the Fe(III) state, exhibiting absorbance maxima at 403.5, 540 (shoulder) and 627 nm. The ferrous and carbonmonoxyferrous states resemble those of haemoglobin, showing maxima at 431.5 and 558 nm, and 421, 542 and 566 nm respectively. Upon aerobic addition of NAD(P)H, the ferric state is reduced to the oxygenated Fe(II) state, characterized by maxima at 413, 544 and 580 nm. This oxy form is not stable and slowly decays to the ferric state. Addition of dithionite and nitrite to the ferric protein results in the formation of a nitrosyl complex, whose e.p.r. characteristics indicate that the b-type haem is attached to the protein through a nitrogenous ligand, probably originating from a histidine residue.

Cited by

References

  1. Biochim Biophys Acta. 1976 Feb 13;422(2):260-72 - PubMed
  2. J Biol Chem. 1980 Aug 25;255(16):7876-82 - PubMed
  3. Biochim Biophys Acta. 1979 May 9;546(2):334-40 - PubMed
  4. FEBS Lett. 1992 May 18;302(3):247-52 - PubMed
  5. Mol Gen Genet. 1991 Apr;226(1-2):49-58 - PubMed
  6. Nature. 1986 Jul 31-Aug 6;322(6078):481-3 - PubMed
  7. J Biol Chem. 1972 Apr 25;247(8):2447-55 - PubMed
  8. Eur J Biochem. 1973 Nov 15;39(2):581-90 - PubMed
  9. Biochim Biophys Acta. 1984 Dec 17;768(3-4):293-317 - PubMed
  10. J Biol Chem. 1982 Apr 10;257(7):3606-17 - PubMed
  11. Anal Biochem. 1978 Jun 15;87(1):206-10 - PubMed
  12. Methods Enzymol. 1978;52:157-66 - PubMed
  13. Biol Met. 1991;4(2):119-25 - PubMed
  14. J Gen Microbiol. 1986 Jun;132(6):1525-39 - PubMed
  15. Adv Biophys. 1970;1:157-82 - PubMed
  16. Nature. 1970 Aug 15;227(5259):680-5 - PubMed
  17. Biochim Biophys Acta. 1979 Feb 26;576(2):471-8 - PubMed

Substances

MeSH terms

Publication Types

LinkOut - more resources