Three-dimensional structure determination using multiple-scattering analysis of XAFS: applications to metalloproteins and coordination chemistry

Levina, Aviva; Armstrong, Robert S.; Lay, Peter A.

doi:10.1016/j.ccr.2004.10.008

Cited by 88 publications

(85 citation statements)

References 93 publications

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“…The slightly lower edge energy of O 2 -␣Hb⅐AHSP compared with free O 2 -␣Hb suggests a lengthening of the Fe-O 2 bond in the AHSP complex. EXAFS data obtained from O 2 -␣Hb and O 2 -␣Hb⅐AHSP were fitted to models for the iron sites using restrained and constrained multiple-scattering models (58,(63)(64)(65). The observed and calculated EXAFS and the corresponding Fourier transforms are shown for O 2 -␣Hb and O 2 -␣Hb⅐AHSP in Fig.…”

Section: Comparison Of the Iron-ligand Structures In O 2 -␣Hb And O 2mentioning

confidence: 99%

“…To probe the electronic structure and coordination environment around the heme iron more directly, we acquired x-ray absorption spectra at the iron K-edge for the physiologically more relevant O 2 -␣Hb and O 2 -␣Hb⅐AHSP complexes. Spectra were recorded at 10 K to minimize photo-damage and increase the importance of multiple-scattering contributions to the EXAFS (58,59). Samples were prepared in buffer containing 0.88 M sucrose, which allowed the formation of a homogeneous glass upon freezing (59).…”

Section: Comparison Of the Iron-ligand Structures In O 2 -␣Hb And O 2mentioning

confidence: 99%

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α-Hemoglobin-stabilizing Protein (AHSP) Perturbs the Proximal Heme Pocket of Oxy-α-hemoglobin and Weakens the Iron-Oxygen Bond

Dickson

Rich

d’Avigdor

et al. 2013

Journal of Biological Chemistry

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Background: ␣-Hemoglobin stabilizing protein (AHSP) is a hemoglobin chaperone. Results: AHSP causes a subtle perturbation of the proximal heme pocket of O 2 -␣-hemoglobin, lengthening the Fe-O 2 bond and enhancing O 2 dissociation. Conclusion: Pro-30 in wild-type AHSP promotes ␣Hb autooxidation by introducing strain into the proximal heme pocket. Significance: ␣Hb⅐AHSP complexes are intermediates in Hb assembly and achieve ␣Hb detoxification.

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Section: Comparison Of the Iron-ligand Structures In O 2 -␣Hb And O 2mentioning

confidence: 99%

Section: Comparison Of the Iron-ligand Structures In O 2 -␣Hb And O 2mentioning

confidence: 99%

α-Hemoglobin-stabilizing Protein (AHSP) Perturbs the Proximal Heme Pocket of Oxy-α-hemoglobin and Weakens the Iron-Oxygen Bond

Dickson

Rich

d’Avigdor

et al. 2013

Journal of Biological Chemistry

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“…These spectroscopic methods are well suited for characterizing the coordination structure of active sites centres of metalloproteins (Strange et al, 2005;PennerHahn, 2005;Levina et al, 2005;Strange & Feiters, 2008). An elegant aspect of X-ray spectroscopy is that the metal centre of interest functions as both the source and the detector of its local chemical environment.…”

Section: Time-resolved X-ray Absorption Spectroscopymentioning

confidence: 99%

Time-resolved structural studies of protein reaction dynamics: a smorgasbord of X-ray approaches

et al. 2010

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Proteins undergo conformational changes during their biological function. As such, a high-resolution structure of a protein's resting conformation provides a starting point for elucidating its reaction mechanism, but provides no direct information concerning the protein's conformational dynamics. Several X-ray methods have been developed to elucidate those conformational changes that occur during a protein's reaction, including time-resolved Laue diffraction and intermediate trapping studies on three-dimensional protein crystals, and timeresolved wide-angle X-ray scattering and X-ray absorption studies on proteins in the solution phase. This review emphasizes the scope and limitations of these complementary experimental approaches when seeking to understand protein conformational dynamics. These methods are illustrated using a limited set of examples including myoglobin and haemoglobin in complex with carbon monoxide, the simple light-driven proton pump bacteriorhodopsin, and the superoxide scavenger superoxide reductase. In conclusion, likely future developments of these methods at synchrotron X-ray sources and the potential impact of emerging X-ray free-electron laser facilities are speculated upon.

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“…[61] The principles for XAS are outlined briefly; however, the reader is referred to reviews for a more detailed description. [58,[62][63][64][65] An X-ray absorption spectrum is generated by subjecting the sample to a tuneable X-ray beam produced by a synchrotron source. The Xray beam energy is swept across an energy range that encompasses the binding energy of the element of interest.…”

Section: X-ray Absorption Spectroscopymentioning

confidence: 99%

Synchrotron Radiation Spectroscopic Techniques as Tools for the Medicinal Chemist: Microprobe X-Ray Fluorescence Imaging, X-Ray Absorption Spectroscopy, and Infrared Microspectroscopy

Dillon

2012

Aust. J. Chem.

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. (2012). Synchrotron radiation spectroscopic techniques as tools for the medicinal chemist: microprobe X-Ray fluorescence imaging, X-Ray absorption spectroscopy, and infrared microspectroscopy. Australian Journal of Chemistry: an international journal for chemical science, 65 (3), 204-217. Synchrotron radiation spectroscopic techniques as tools for the medicinal chemist: microprobe X-Ray fluorescence imaging, X-Ray absorption spectroscopy, and infrared microspectroscopy AbstractThis review updates the recent advances and applications of three prominent synchrotron radiation techniques, microprobe X-ray fluorescence spectroscopy/imaging, X-ray absorption spectroscopy, and infrared microspectroscopy, and highlights how these tools are useful to the medicinal chemist. A brief description of the principles of the techniques is given with emphasis on the advantages of using synchrotron radiation-based instrumentation rather than instruments using typical laboratory radiation sources. This review focuses on several recent applications of these techniques to solve inorganic medicinal chemistry problems, focusing on studies of cellular uptake, distribution, and biotransformation of established and potential therapeutic agents. The importance of using these synchrotron-based techniques to assist the development of, or validate the chemistry behind, drug design is discussed. AbstractThis review updates the recent advances and applications of three prominent synchrotron radiation techniques, microprobe X-ray fluorescent spectroscopy/imaging, X-ray absorption spectroscopy and infrared microspectroscopy, and highlights how these tools are useful to the medicinal chemist. A brief description of the principles of the techniques is given with emphasis on the advantages of using synchrotron radiation-based instrumentation rather than instruments using typical laboratory radiation sources. This review focuses on a number of recent applications of these techniques to solve inorganic medicinal chemistry problems, focusing on studies of cellular uptake, distribution and biotransformation of established and potential therapeutic agents. The importance of using these synchrotron-based techniques to assist the development, or validate the chemistry behind, drug design is discussed.3

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Three-dimensional structure determination using multiple-scattering analysis of XAFS: applications to metalloproteins and coordination chemistry

Cited by 88 publications

References 93 publications

α-Hemoglobin-stabilizing Protein (AHSP) Perturbs the Proximal Heme Pocket of Oxy-α-hemoglobin and Weakens the Iron-Oxygen Bond

α-Hemoglobin-stabilizing Protein (AHSP) Perturbs the Proximal Heme Pocket of Oxy-α-hemoglobin and Weakens the Iron-Oxygen Bond

Time-resolved structural studies of protein reaction dynamics: a smorgasbord of X-ray approaches

Synchrotron Radiation Spectroscopic Techniques as Tools for the Medicinal Chemist: Microprobe X-Ray Fluorescence Imaging, X-Ray Absorption Spectroscopy, and Infrared Microspectroscopy

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