X-ray crystal structure of the ferric sperm whale myoglobin: Imidazole complex at 2.0 Å resolution

Lionetti, Claudia; Guanziroli, Maria Grazia; Frigerio, Francesco; Ascenzi, Paolo; Bolognesi, Martino

doi:10.1016/0022-2836(91)90744-q

Cited by 64 publications

(50 citation statements)

References 20 publications

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“…For a comparison between soybean Lb a nicotinate and myoglobin (Mb) we use a crystallographically characterized derivative of Mb with a bulky exogenous ligand, the sperm whale Mb:imidazole complex (Lionetti, Guanziroli, Frigerio, Ascenzi & Bolognesi, 1991). A superposition of their C '~ atoms shows that Lb has a significantly larger distal heme cavity than Mb (Fig.…”

Section: The Heme Group and Heme Cavitymentioning

confidence: 99%

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Structure of Ferric Soybean LeghemoglobinaNicotinate at 2.3 Å Resolution

Ellis¹,

Appleby²,

Guss³

et al. 1997

Acta Cryst D

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Soybean leghemoglobin a is a small (16 kDa) protein facilitating the transport of Oz to respiring N2-fixing bacteria at low free-O2 tension. The crystal structure of soybean ferric leghemoglobin a nicotinate has been refined at 2.3 A resolution. The final R factor is 15.8% for 6877 reflections between 6.0 and 2.3 ~. The structure of soybean leghemoglobin a (143 residues) is closely similar to that of lupin leghemoglobin II (153 residues), the proteins having 82 identical residues when the sequences are aligned. The new structure provides support for the conclusion that the unique properties of leghemoglobin arise principally from a heme pocket considerably larger and more flexible than that of myoglobin, a strongly ruffled heme group, and a proximal histidine orientation more favourable to ligand binding.

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Section: The Heme Group and Heme Cavitymentioning

confidence: 99%

“…The largest value of F found in any Mb structure is 20 °. It occurs in the structure of the ferric Mb:imidazole complex (Lionetti et al, 1991). Fig.…”

Section: The Heme Group and Heme Cavitymentioning

confidence: 99%

Structure of Ferric Soybean LeghemoglobinaNicotinate at 2.3 Å Resolution

Ellis¹,

Appleby²,

Guss³

et al. 1997

Acta Cryst D

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“…10 The X-ray data of metMb(Im) demonstrated that the heme active site structure is substantially altered by the coordination of bulky Im and that the Fe 3þ -Im coordination structure in the protein is largely distorted compared to those in model compounds. 11 The distorted Fe 3þ -Im coordination structure is possibly responsible for the thermal spin equilibrium of metMb(Im). Consequently, the predominance of the low-spin state in heme-DNA(Im) dictated that the Fe 3þ -Im coordination structure is not significantly distorted.…”

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Exogenous Ligand Binding Property of a Heme–DNA Coordination Complex

et al. 2006

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“…Several studies in past years have revealed consistent differences between the structure of the heme in globins and peroxidases [31]. As shown from XAS and high resolution X-ray structures, globins typically have an Fe−N h distance of about 2.1 Å while in the peroxidases this distance is typically shorter by about 0.2 Å, resulting in a typical Fe−N h distance of about 1.9 Å [31][32][33][34][35][36][37][38] (see also Table 3). This was proposed to be crucial to explain the different reactivity observed between the two groups of proteins [34,35].…”

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confidence: 99%

“…The globins, typified by h-Mb, lack this strong hydrogen bonding to the proximal histidine and exhibit a longer Fe−N h bond. Moreover, the orientation of the imidazole plane with respect to the pyrrole nitrogen plane is such that the proximal histidine is in a fully eclipsed rotameric conformation that precludes optimal overlap of the iron axial and histidine nitrogen orbitals [36,37].…”

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confidence: 99%

Unusual proximal heme pocket geometry in the deoxygenated Thermobifida fusca: A combined spectroscopic investigation

Arcovito¹,

Bonamore²,

Hazemann³

et al. 2010

Biophysical Chemistry

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The spectroscopic properties of the deoxygenated truncated hemoglobin from the actinobacterium Thermobifida fusca have been investigated by means of extended X-ray absorption fine structure (EXAFS), X-ray absorption near edge structure (XANES), and near infrared spectroscopies both at room and cryogenic temperatures. At room temperature the near infrared charge transfer band III occurs at 772 nm, a value that is unusually high for a canonical deoxygenated hemoglobin species, and can only be found as a transient species after photolysis in vertebrate hemoglobins and myoglobins or under strongly dehydrating conditions. EXAFS and XANES quantitative analyses, carried out in parallel with deoxygenated horse myoglobin, revealed an unusually short iron-histidine distance 1.90 +/- 0.03 angstrom, significantly shorter than the deoxygenated horse myoglobin distance of 2.11 +/- 0.02 angstrom. These findings provide novel structural basis for discussing the fine structural geometry of the proximal site, and eventually mapping the coordinates of the metal with respect to the pyrrole nitrogens and the proximal histidine nitrogen. (C) 2009 Elsevier B.V. All rights reserved

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X-ray crystal structure of the ferric sperm whale myoglobin: Imidazole complex at 2.0 Å resolution

Cited by 64 publications

References 20 publications

Structure of Ferric Soybean LeghemoglobinaNicotinate at 2.3 Å Resolution

Structure of Ferric Soybean LeghemoglobinaNicotinate at 2.3 Å Resolution

Exogenous Ligand Binding Property of a Heme–DNA Coordination Complex

Unusual proximal heme pocket geometry in the deoxygenated Thermobifida fusca: A combined spectroscopic investigation

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