Deciphering the Structural Role of Histidine 83 for Heme Binding in Hemophore HasA

Caillet‐Saguy, Célia; Turano, Paola; Piccioli, Mario; Lukat-Rodgers, Gudrun S.; Czjzek, Mirjam; Guigliarelli, Bruno; Izadi-Pruneyre, Nadia; Rodgers, Kenton R.; Delepierre, Muriel; Lecroisey, Anne

doi:10.1074/jbc.m703795200

Cited by 47 publications

(48 citation statements)

References 61 publications

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“…This is confirmed by the corresponding high-frequency RR spectrum ( for ferric Ph-2/2HbO at pH 7.6 [13] where, probably due to different preparation procedures, multiple LS forms were observed (see Materials and methods). However, as reported in that case, the absorption maxima of the LS form are quite unusual, and reminiscent of those of ferric Chlamydomonas chloroplast Hb [23] and of the hemophore HasA proteins from Serratia marcescens and Pseudomonas aeruginosa [24,25]. Nevertheless, they are very different from either a LS His-Fe-His (that exhibits well defined absorption bands at about 535 and 565 nm) or a His-Fe-OH heme complex as observed at alkaline pH (see below) [26].…”

Section: Spectroscopic Measurements In Solutionmentioning

confidence: 93%

Structural flexibility of the heme cavity in the cold‐adapted truncated hemoglobin from the Antarctic marine bacterium Pseudoalteromonas haloplanktis TAC125

et al. 2015

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*These authors contributed equally to this workTruncated hemoglobins build one of the three branches of the globin protein superfamily. They display a characteristic two-on-two a-helical sandwich fold and are clustered into three groups (I, II and III) based on distinct structural features. Truncated hemoglobins are present in eubacteria, cyanobacteria, protozoa and plants. Here we present a structural, spectroscopic and molecular dynamics characterization of a group-II truncated hemoglobin, encoded by the PSHAa0030 gene from Pseudoalteromonas haloplanktis TAC125 (Ph-2/2HbO), a cold-adapted Antarctic marine bacterium hosting one flavohemoglobin and three distinct truncated hemoglobins. The Ph-2/2HbO aquo-met crystal structure (at 2.21A resolution) shows typical features of group-II truncated hemoglobins, namely the twoon-two a-helical sandwich fold, a helix Φ preceding the proximal helix F, and a heme distal-site hydrogen-bonded network that includes water molecules and several distal-site residues, including His(58)CD1. Analysis of Ph-2/2HbO by electron paramagnetic resonance, resonance Raman and electronic absorption spectra, under varied solution conditions, shows that Ph-2/2HbO can access diverse heme ligation states. Among these, detection of a low-spin heme hexa-coordinated species suggests that residue Tyr(42)B10 can undergo large conformational changes in order to act as the sixth heme-Fe ligand. Altogether, the results show that Ph-2/2HbO maintains the general structural features of group-II truncated hemoglobins but displays enhanced conformational flexibility in the proximity of the heme cavity, a property probably related to the functional challenges, such as low Abbreviations 5c, penta-coordinated heme state; 6c, hexa-coordinated heme state; At-2/2HbO, TrHbII from Agrobacterium tumefaciens; Ath-2/2HbO,

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Section: Spectroscopic Measurements In Solutionmentioning

confidence: 93%

Structural flexibility of the heme cavity in the cold‐adapted truncated hemoglobin from the Antarctic marine bacterium Pseudoalteromonas haloplanktis TAC125

et al. 2015

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“…The wavelength maxima suggest the presence of various species, namely a His-Fe-H 2 O six-coordinate high-spin (6cHS) form [bands at 503 and charge-transfer transition (CT1) at 635 nm] and at least one 6c-low-spin (LS) heme (bands at 533 and 570 nm). The absorption maxima of the LS forms are quite unusual, reminiscent of those of ferric Chlamydomonas Hb [20] and the hemophore HasA proteins from Serratia marcescens and Pseudomonas aeruginosa [21,22], and they are very different from either a LS His-Fe-His (that exhibits well-defined absorption bands at about 535 and 565 nm) or a His-Fe-OH heme complex (that exhibits well-defined absorption bands at about 540 and 580 nm) [23]. Therefore, on the basis of the similarity with the UV-vis spectrum of ferric Chlamydomonas Hb and HasA hemophores, a His and a Tyr ligand are suggested to occupy the fifth and sixth coordination positions, respectively.…”

Section: Spectroscopy At Room Temperaturementioning

confidence: 99%

The peculiar heme pocket of the 2/2 hemoglobin of cold-adapted Pseudoalteromonas haloplanktis TAC125

et al. 2010

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The genome of the cold-adapted bacterium Pseudoalteromonas haloplanktis TAC125 contains multiple genes encoding three distinct monomeric hemoglobins exhibiting a 2/2 a-helical fold. In the present work, one of these hemoglobins is studied by resonance Raman, electronic absorption and electronic paramagnetic resonance spectroscopies, kinetic measurements, and different bioinformatic approaches. It is the first cold-adapted bacterial hemoglobin to be characterized. The results indicate that this protein belongs to the 2/2 hemoglobin family, Group II, characterized by the presence of a tryptophanyl residue on the bottom of the heme distal pocket in position G8 and two tyrosyl residues (TyrCD1 and TyrB10). However, unlike other bacterial hemoglobins, the ferric state, in addition to the aquo hexacoordinated high-spin form, shows multiple hexacoordinated low-spin forms, where either TyrCD1 or TyrB10 can likely coordinate the iron. This is the first example in which both TyrCD1 and TyrB10 are proposed to be the residues that are alternatively involved in heme hexacoordination by endogenous ligands.

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“…Such systems have been described in pathogens such as Escherichia coli (Otto et al 2005, Suits et al 2006Suits et al 2009;Hagan and Mobley 2009); Vibrio cholerae (Mey and Payne 2001;Wyckoff et al 2004;Wyckoff et al 2006;Wyckoff et al 2007); Shigella (Mills and Payne 1995;Mills and Payne 1997;Wyckoff et al 2005); Pseudomonas aeruginosa (Vasil and Ochsner 1999;Tong and Guo 2007;Vasil 2007;Yukl et al 2010;Jepkorir et al 2010;Cornelis 2010); Serratia marcescens Izadi-Pruneyre et al 2006;Czjzek et al 2007;Benevides-Matos et al 2008;Letoffe et al 2008;Caillet-Saguy et al 2008); Yersinia pestis (Thompson et al 1999;Rossi et al 2001;Perry et al 2003;Mattle et al 2010) and Legionella pneumophila Pope et al 1996). Heme uptake in Gram-positive bacteria is less well studied.…”

Section: Introductionmentioning

confidence: 95%

Mechanisms of iron import in anthrax

Honsa

Maresso

2011

Biometals

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During an infection, bacterial pathogens must acquire iron from the host to survive. However, free iron is sequestered in host proteins, which presents a barrier to iron-dependent bacterial replication. In response, pathogens have developed mechanisms to acquire iron from the host during infection. Interestingly, a significant portion of the iron pool is sequestered within heme, which is further bound to host proteins such as hemoglobin. The copious amount of heme-iron makes hemoglobin an ideal molecule for targeted iron uptake during infection. While the study of heme acquisition is well represented in Gram-negative bacteria, the systems and mechanism of heme uptake in Gram-positive bacteria has only recently been investigated. Bacillus anthracis, the causative agent of anthrax disease, represents an excellent model organism to study iron acquisition processes owing to a multifaceted lifecycle consisting of intra- and extracellular phases and a tremendous replicative potential upon infection. This review provides an in depth description of the current knowledge of B. anthracis iron acquisition and applies these findings to a general understanding of how pathogenic Gram-positive bacteria transport this critical nutrient during infection.

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Deciphering the Structural Role of Histidine 83 for Heme Binding in Hemophore HasA

Cited by 47 publications

References 61 publications

Structural flexibility of the heme cavity in the cold‐adapted truncated hemoglobin from the Antarctic marine bacterium Pseudoalteromonas haloplanktis TAC125

Structural flexibility of the heme cavity in the cold‐adapted truncated hemoglobin from the Antarctic marine bacterium Pseudoalteromonas haloplanktis TAC125

The peculiar heme pocket of the 2/2 hemoglobin of cold-adapted Pseudoalteromonas haloplanktis TAC125

Mechanisms of iron import in anthrax

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