Heteronuclear Magnetic Resonance Applications to Biological and Related Paramagnetic Molecules

Mispelter, Joël; Momenteau, M.; Lhoste, Jean‐Marc

doi:10.1007/978-1-4615-2886-9_6

Cited by 24 publications

(32 citation statements)

References 126 publications

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“…Thus, the corresponding shifts are located at about 200 ppm for C β carbons, approximately 100 ppm for C α carbons, and about 70 ppm for C m carbons (Fig. 10a) [23,72]. By comparison spin delocalization in ferrihemes with the less common S=1/2, (d xy ) 1 electronic configuration is mainly into the 3a 2u (π) orbital [15], which exhibits large electron density at the C m carbons and small electron density at the C α and C β carbons (Fig.…”

Section: Nmr Chemical Shifts Of Quaternary Carbons and Heme Electromentioning

confidence: 95%

“…6) [20]. S C accounts for spin polarization of the 1 s orbital by unpaired spin density located on the p z (π) orbital of the same carbon atom, Q Cxi accounts for spin polarization of the 2 s orbitals on neighboring carbons by unpaired π spin density on the observed carbon atom, and Q xiC for spin polarization of the 2 s electrons on the observed carbon atom by π spin density on the neighboring carbons [17,21,22,23,24].…”

Section: Mario Rivera · Gregori a Caignanmentioning

confidence: 99%

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Recent developments in the 13 C NMR spectroscopic analysis of paramagnetic hemes and heme proteins

Rivera

Caignan

2004

Analytical and Bioanalytical Chemistry

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Despite the wealth of information that has been obtained from the study of paramagnetic hemes and heme proteins by 1H NMR spectroscopy, there are certain limitations imposed by the nature of paramagnetically affected resonances that are difficult to overcome. Although it has long been recognized that 13C NMR spectroscopy is likely to be a powerful complementary technique to overcome some of these limitations, the low sensitivity and low natural abundance of 13C nuclei has resulted in a lag in the application of 13C NMR spectroscopy to the study of paramagnetic hemes and heme proteins. The tremendous advances in methodology and instrumentation witnessed in the NMR field, coupled to the advent of recombinant DNA methods that have made possible the preparation and purification of significant quantities of proteins, and the biosynthesis of 13C-labeled heme, have contributed to an increased interest in the study of paramagnetic heme active sites by 13C NMR spectroscopy. As a consequence, 13C NMR spectroscopy is emerging as a powerful tool to study heme electronic structure and structure-function relationships in heme-containing proteins. In this report we strive to summarize some of the recent developments in the analysis of paramagnetic hemes and heme-containing proteins by 13C NMR spectroscopy.

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Section: Nmr Chemical Shifts Of Quaternary Carbons and Heme Electromentioning

confidence: 95%

Section: Mario Rivera · Gregori a Caignanmentioning

confidence: 99%

Recent developments in the 13 C NMR spectroscopic analysis of paramagnetic hemes and heme proteins

Rivera

Caignan

2004

Analytical and Bioanalytical Chemistry

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“…4(b) [90]; smaller spin density is expected at the a-pyrrole carbons and negligible spin density at the meso carbons. As a consequence, low-spin d p ferrihemes exhibit meso carbon resonances near 70 ppm [100,101]. The 422 ppm chemical shift obtained from the 13 C NMR spectrum of [meso-13 C-TPPFe(OCH 3 )(OO t Bu)] À was therefore interpreted to suggest a significant population of the (d xy ) 1 electron configuration at 218 K [82].…”

Section: Increasing the Reactivity Of The Heme Macrocycle To Activelymentioning

confidence: 98%

Heme oxygenase, steering dioxygen activation toward heme hydroxylation

Rivera

Zeng

2005

Journal of Inorganic Biochemistry

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“…Finally, w I and w S are the Larmor frequencies of the nuclear spin, I, and the electron spin, S, respectively. The correlation times, t c,1 and t c,2 are given by [52] …”

Section: Paramagnetic Metal Ionsmentioning

confidence: 99%

Investigating metal-binding in proteins by nuclear magnetic resonance

Jensen

Hass

Hansen

et al. 2007

Cell. Mol. Life Sci.

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Metal ions play a key role for the function of many proteins. The interaction of the metal ion with the protein and its involvement in the function of the protein vary widely. In some proteins, the metal ion is bound tightly to the ligand residues and may be the key player in the function of the protein, as in the case of blue copper proteins. In other proteins, the metal ion is bound only temporarily and loosely to the protein, as in the case of some metalloenzymes and other proteins where the metal ion acts as a cofactor necessary for the function of the protein. Such proteins are often known as metal ion-activated proteins. The review focuses on recent nuclear magnetic resonance (NMR) studies of a series of metal-dependent proteins and the characterization of the metal-binding sites. In particular, we focus on NMR techniques for studying metal binding to proteins such as chemical shift mapping, paramagnetic NMR and changes in backbone dynamics upon metal binding.

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Heteronuclear Magnetic Resonance Applications to Biological and Related Paramagnetic Molecules

Cited by 24 publications

References 126 publications

Recent developments in the 13 C NMR spectroscopic analysis of paramagnetic hemes and heme proteins

Recent developments in the 13 C NMR spectroscopic analysis of paramagnetic hemes and heme proteins

Heme oxygenase, steering dioxygen activation toward heme hydroxylation

Investigating metal-binding in proteins by nuclear magnetic resonance

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