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 language | English (US) |
|---|---|
| Pages (from-to) | 255-286 |
| Number of pages | 32 |
| Journal | Methods in Enzymology |
| Volume | 437 |
| DOIs | |
| State | Published - 2008 |
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ASJC Scopus subject areas
- Biochemistry
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Hemoglobins from Mycobacterium tuberculosis and Campylobacter jejuni : A Comparative Study with Resonance Raman Spectroscopy. / Lu, Changyuan; Egawa, Tsuyoshi; Mukai, Masahiro; Poole, Robert K.; Yeh, Syun-Ru.
In: Methods in Enzymology, Vol. 437, 2008, p. 255-286.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Hemoglobins from Mycobacterium tuberculosis and Campylobacter jejuni
T2 - A Comparative Study with Resonance Raman Spectroscopy
AU - Lu, Changyuan
AU - Egawa, Tsuyoshi
AU - Mukai, Masahiro
AU - Poole, Robert K.
AU - Yeh, Syun-Ru
PY - 2008
Y1 - 2008
N2 - 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.
AB - 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.
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UR - http://www.scopus.com/inward/citedby.url?scp=47049122888&partnerID=8YFLogxK
U2 - 10.1016/S0076-6879(07)37014-6
DO - 10.1016/S0076-6879(07)37014-6
M3 - Article
VL - 437
SP - 255
EP - 286
JO - Methods
JF - Methods
SN - 1046-2023
ER -