NMR Spectroscopy of Paramagnetic Haem Proteins

Satterlee, James D.

doi:10.1016/s0066-4103(08)60235-5

Cited by 91 publications

(85 citation statements)

References 181 publications

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“…The properties of these resonances are collected in table 1. The range of shifts displayed in these experiments is consistent with their assignment to a low spin ferric haem [14]. All the resonance shifts show a linear inverse dependence on temperature.…”

Section: Resultssupporting

confidence: 86%

“…Haem a3 is high spin in the ferric (S = 5/2) and ferrous (S = 2) states, but some inhibitors of oxidase activity, such as cyanide or carbon monoxide, bind to this haem making it low spin [5,6]. Many proteins which contain haem groups in paramagnetic (S # 0) states give rise to paramagnetically shifted resonances in 'H NMR spectra [14]. The spectra of proteins containing isolated copper ions do not show such features; usually resonances of nuclei close to cupric centres are considerably broadened due to the magnetic properties of the metal ion [19].…”

Section: Resultsmentioning

confidence: 99%

“…Proton nuclear magnetic resonance ('H NMR) spectroscopy has been successfully employed in many studies of a variety of haem proteins [14], but only one such study of cytochrome oxidase has been reported [ 151. This paper describes preliminary 'H NMR studies of dimeric and monomeric bovine heart cytochrome oxidase, and shows the detection of paramagnetically shifted resonances from haem a.…”

Section: Introductionmentioning

confidence: 99%

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A ¹H NMR study of bovine cytochrome oxidase

et al. 1989

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Section: Resultssupporting

confidence: 86%

Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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A ¹H NMR study of bovine cytochrome oxidase

et al. 1989

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“…1H NMR spectra are very sensitive to the axial ligation state in low-spin heme-proteins (37). We have already reported that the pattern of hyperfine-shifted resonances of heme-Hx is species dependent (15).…”

mentioning

confidence: 99%

Roles of heme iron-coordinating histidine residues of human hemopexin expressed in baculovirus-infected insect cells.

Satoh

Satoh²,

Iwahara³

et al. 1994

Proc. Natl. Acad. Sci. U.S.A.

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Hemopexin (Hx), the major heme-binding plasma glycoprotein, scavenges circulating heme and performs an antioxidant function. In the present study, human Hx was expressed in a baculovirus system and its presumed essential His residues were mutated to Thr as a means of investigating their participation in heme binding. The recombinant Hx proteins were purified by sequential chromatography on Con A-agarose and SP-Sepharose. The purified recombinant wild-type Hx retained its heme binding. The binding constant for heme was considerably reduced, however, suggesting that glycosylation contributes critically to the heme binding property of Hx. Mutation either at His-127 or at His-56 plus His-127, but not at His-56 per se, reduced the affinity for heme by an order of magnitude relative to wild-type Hx. It is concluded that His-127 contributes to the high affinity for heme. We recorded proton NMR spectra to investigate the possibility that the degree of high-spin content is increased by deletion of an axial His-iron coordination. 1H NMR data indicate that each of the single-mutant heme-Hx complexes is predominantly low-spin, perhaps owing to coordination of the heme iron by the Thr side-chain oxygen or water oxygen coordinating to the iron.

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“…(Satterlee, 1986). 까Ie potential of lH NMR in these systems has been increased dramatically by the application ofmulti 김imensional methods (peyton, 1991; Yu et aI., 1990), although not yet for a paramagnetic molecule as large as hemeeHx.…”

Section: Discussionmentioning

confidence: 99%

Nuclear Magnetic Resonance Investigation of the Interaction of Heme Binding Proteins with SnIVprotoporphyrin IX and Heme: Structure and Conformational Changes of Myoglobin and Hemopexin

Deeb

2000

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NMR Spectroscopy of Paramagnetic Haem Proteins

Cited by 91 publications

References 181 publications

A ¹H NMR study of bovine cytochrome oxidase

A ¹H NMR study of bovine cytochrome oxidase

Roles of heme iron-coordinating histidine residues of human hemopexin expressed in baculovirus-infected insect cells.

Nuclear Magnetic Resonance Investigation of the Interaction of Heme Binding Proteins with SnIVprotoporphyrin IX and Heme: Structure and Conformational Changes of Myoglobin and Hemopexin

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NMR Spectroscopy of Paramagnetic Haem Proteins

Cited by 91 publications

References 181 publications

A 1H NMR study of bovine cytochrome oxidase

A 1H NMR study of bovine cytochrome oxidase

Roles of heme iron-coordinating histidine residues of human hemopexin expressed in baculovirus-infected insect cells.

Nuclear Magnetic Resonance Investigation of the Interaction of Heme Binding Proteins with SnIVprotoporphyrin IX and Heme: Structure and Conformational Changes of Myoglobin and Hemopexin

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A ¹H NMR study of bovine cytochrome oxidase

A ¹H NMR study of bovine cytochrome oxidase