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Truncated Hemoglobins: A New Family of Hemoglobins Widely Distributed in Bacteria, Unicellular Eukaryotes, and Plants* 210
TLDR
Crystal structures show that trHb tertiary structure is based on a 2-on-2 -hel-ical sandwich, which represents an unprecedented editing of the highly conserved globin fold, and may provide a path for ligand diffusion to the heme. Expand
A novel two‐over‐two α‐helical sandwich fold is characteristic of the truncated hemoglobin family
TLDR
Crystal structures of trHbs from the ciliated protozoan Paramecium caudatum and the green unicellular alga Chlamydomonas eugametos show that the tertiary structure of both proteins is based on a ‘two‐over‐two’ α‐helical sandwich, reflecting an unprecedented editing of the classical ‘three‐ over‐three’α‐helICAL globin fold. Expand
Mycobacterium tuberculosis hemoglobin N displays a protein tunnel suited for O2 diffusion to the heme
TLDR
It is proposed that in trHbN, heme Fe/O2 stereochemistry and the protein matrix tunnel may promote O2/NO chemistry in vivo, as a M.tuberculosis defense mechanism against macrophage nitrosative stress. Expand
A cooperative oxygen-binding hemoglobin from Mycobacterium tuberculosis.
TLDR
The results suggest that, physiologically, the primary role of HbN may be to protect the bacilli against reactive nitrogen species produced by the host macrophage. Expand
Characterization of the LI818 polypeptide from the green unicellular alga Chlamydomonas reinhardtii
TLDR
It is shown here that, in contrast to CAB polypeptides, LI818Polypeptide is not tightly embedded into the thylakoid membranes and is localized in stroma-exposed regions, which suggests a very ancient origin for this group of polyPEptides. Expand
Truncated hemoglobin HbN protects Mycobacterium bovis from nitric oxide
TLDR
It is reported that disruption of M. bovis bacillus Calmette–Guérin glbN caused a dramatic reduction in the NO-consuming activity of stationary phase cells, and that activity could be restored fully by complementing knockout cells withglbN, and an NO-metabolizing activity in M. tuberculosis or M.bovis is demonstrated. Expand
The Chlamydomonas reinhardtii LI818 gene represents a distant relative of the cabI/II genes that is regulated during the cell cycle and in response to illumination
TLDR
It is shown that in LD synchronized Chlamydomonas cells LI818 mRNA accumulation is subject to dual regulation that involves separable regulation by light and an endogenous oscillator, suggesting that these regulatory mechanisms are mediated by labile proteins. Expand
A TyrCD1/TrpG8 hydrogen bond network and a TyrB10—TyrCD1 covalent link shape the heme distal site of Mycobacterium tuberculosis hemoglobin O
TLDR
Truncated hemoglobins are small hemoproteins, identified in microorganisms and in some plants, forming a separate cluster within the Hb superfamily, and sequence analysis shows that the two proteins share 18% amino acid identities and belong to different groups within the truncated Hb cluster. Expand
Reactions of Mycobacterium tuberculosis truncated hemoglobin O with ligands reveal a novel ligand-inclusive hydrogen bond network.
TLDR
Investigating the reactions of trHbO and mutants using stopped-flow spectrometry, flash photolysis, and UV-enhanced resonance Raman spectroscopy found that changing CD1 or B10 tyrosine for phenylalanine causes only small changes in the rate of O(2) dissociation, suggesting that more than one hydrogen bond must be broken at a time to promote ligand escape. Expand
Ligand interactions in the distal heme pocket of Mycobacterium tuberculosis truncated hemoglobin N: roles of TyrB10 and GlnE11 residues.
TLDR
The findings suggest that the functional processes of ligand binding and diffusion are controlled in trHbN through the dynamic interaction of residues Y(B10), Q(E11), F(E15), and the heme ligand. Expand
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