Spectroscopic investigations of ferric cytochrome P-450-CAM ligand complexes. Identification of the ligand trans to cysteinate in the native enzyme.

Simulations of 14N ESEEM patterns for an S=1/2, I=1 spin system with an isotropic hyperfine coupling, in a nonordered solid are reported. The dependence of the simulated patterns on the quadrupole and hyperfine coupling constants, and on the external field strength is examined and discussed. Three distinct types of powder patterns are identified, all of which exhibit discrete peaks. The dependence of the frequency, width, and amplitude of these peaks on the coupling constants and field strength is elucidated in simple terms. The results provide a basis for the interpretation of ESEEM patterns and for the development of experimental tactics: the variation of field strength (electron spin‐excitation frequency) can be used to manipulate modulation depths, select specific nuclei, and ascertain accurate quadrupole coupling constants. The anisotropy of the amplitude of modulation components, its effect on ESEEM powder patterns, and its implications as regards orientation selection experiments are also considered.

Analysis of 14N ESEEM patterns of randomly oriented solids

Cytochrome c folding was initiated using a new solution mixer that provides a time window which covers over 90% of the burst phase unresolved by conventional stop-flow measurements. Folding was followed by resonance Raman scattering. Kinetic analysis of the high frequency Raman data indicates that a nascent phase occurs within the mixing dead time of 100 microseconds. A significant fraction of the protein was found to be trapped in a misfolded bis-histidine form during the nascent phase at pH 4.5, thereby preventing the protein from folding rapidly and homogeneously. The nascent phase was followed by a haem-ligand exchange phase that populates the native histidine-methionine coordinated form through a thermodynamically controlled equilibrium.

Folding of cytochrome c initiated by submillisecond mixing.

Electron spin resonance (ESR) Spectroscopy has recently undergone a major innovative advance, which is described by the magical phrase pulsed ESR. To the spectroscopist who rubs this Aladdin's lamp there now opens up the mysterious world of spin acrobatics with its many novel and surprising phenomena. The use of pulse techniques makes it possible to reduce measurement times, increase sensitivity, improve resolution and simplify spectra. This article describes the most important pulse techniques used in ESR spectroscopy. Mathematical descriptions are kept to a minimum, space being devoted instead to examples of applications in various areas of chemical research.

Pulsed Electron Spin Resonance Spectroscopy: Basic Principles, Techniques, and Examples of Applications [New Analytical Methods (43)]

Electron spin echo envelope modulation (ESEEM) spectroscopy as a tool to investigate the coordination environment of metal centers

Studies of the electron-nuclear coupling between Fe(III) and 14N in cytochrome P-450 and in a series of low spin heme compounds.

Water coordination by heme iron in metmyoglobin.

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Studies of the electron-nuclear coupling between Fe(III) and 14N in cytochrome P-450 and in a series of low spin heme compounds.

Water coordination by heme iron in metmyoglobin.