Hemoglobins from Mycobacterium tuberculosis and Campylobacter jejuni: A Comparative Study with Resonance Raman Spectroscopy

Changyuan Lu, Tsuyoshi Egawa, Masahiro Mukai, Robert K. Poole, Syun Ru Yeh

Research output: Chapter in Book/Report/Conference proceedingChapter

17 Scopus citations

Abstract

Three groups of hemoglobins (Hbs) have been identified in unicellular organisms: (1) the truncated Hbs (trHb) that display a novel two-over-two α-helical structure, (2) the flavohemoglobins (FHb) that comprise a Hb domain with a classical three-over-three α-helical structure and a covalently attached flavin-containing reductase domain, and (3) the single-domain Hbs (sdHb) that exhibit high sequence homology and structural similarity to the Hb domain of FHb. On the basis of phylogenetic analysis, the trHbs can be further divided into three subgroups: TrHb-I, TrHb-II, and TrHb-III. The various classes of Hbs may coexist in the same organism, suggesting distinct functions for each class of Hb. This chapter reviews the structural and functional properties of a TrHb-I (trHbN) and a TrHb-II (trHbO) from Mycobacterium tuberculosis, as well as a TrHb-III (trCtb) and a sdHb (Cgb) from Campylobacter jejuni on the basis of resonance Raman spectroscopic studies.

Original languageEnglish (US)
Title of host publicationGlobins and Other Nitric Oxide-Reactive Proteins, Part B
PublisherAcademic Press Inc.
Pages255-286
Number of pages32
ISBN (Print)9780123742780
DOIs
StatePublished - Jan 1 2008

Publication series

NameMethods in Enzymology
Volume437
ISSN (Print)0076-6879

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ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

Cite this

Lu, C., Egawa, T., Mukai, M., Poole, R. K., & Yeh, S. R. (2008). Hemoglobins from Mycobacterium tuberculosis and Campylobacter jejuni: A Comparative Study with Resonance Raman Spectroscopy. In Globins and Other Nitric Oxide-Reactive Proteins, Part B (pp. 255-286). (Methods in Enzymology; Vol. 437). Academic Press Inc.. https://doi.org/10.1016/S0076-6879(07)37014-6