Spectroscopy iron proteins

G Backes, Y Mino, TM Loehr, TE Meyer, MA Cusanovich, WV Sweeny, ET Adman, J Sand-ers-Loehr. The environment of Ee4S4 clusters in ferredoxms and high-potential iron proteins. New information from X-ray crystallography and resonance Raman spectroscopy. J Am Chem Soc 113 2055-2064, 1991. 

Probing Metalloproteins Electronic absorption spectroscopy of copper proteins, 226, 1 electronic absorption spectroscopy of nonheme iron proteins, 226, 33 cobalt as probe and label of proteins, 226, 52 biochemical and spectroscopic probes of mercury(ii) coordination environments in proteins, 226, 71 low-temperature optical spectroscopy metalloprotein structure and dynamics, 226, 97 nanosecond transient absorption spectroscopy, 226, 119 nanosecond time-resolved absorption and polarization dichroism spectroscopies, 226, 147 real-time spectroscopic techniques for probing conformational dynamics of heme proteins, 226, 177 variable-temperature magnetic circular dichroism, 226, 199 linear dichroism, 226, 232 infrared spectroscopy, 226, 259 Fourier transform infrared spectroscopy, 226, 289 infrared circular dichroism, 226, 306 Raman and resonance Raman spectroscopy, 226, 319 protein structure from ultraviolet resonance Raman spectroscopy, 226, 374 single-crystal micro-Raman spectroscopy, 226, 397 nanosecond time-resolved resonance Raman spectroscopy, 226, 409 techniques for obtaining resonance Raman spectra of metalloproteins, 226, 431 Raman optical activity, 226, 470 surface-enhanced resonance Raman scattering, 226, 482 luminescence... 

Bearden, A. J., T. II. Moss, R. G. Bartsch, and M. A. Cusanovitch Mossbauer spectroscopy studies of Chromatium non-heme iron proteins. In Non-Heme Iron Proteins Role in Energy Conversion, A. San Pietro, ed., Antioch Press, Yellow Springs, Ohio, pp. 87—99 (1965). 

The electron-transport chain contains a number of iron-sulfur proteins (also known as nonheme iron proteins). The iron atoms are bound to the proteins via cysteine —S— groups and sulfide ions one such 4-Fe cluster is shown in Fig. 14-1. These proteins mediate electron transport by direct electron transfer changes in oxidation state of the iron in iron-sulfur proteins can be monitored by electron spin resonance spectroscopy (ESR). 

Beinert, H. EPR spectroscopy in the detection, study and identification of protein-bound non-heme iron. In Non-heme iron proteins, p. 23 A. San Pietro, ed. Yellow Springs, Ohio Antioch Press 1965. 

It was suggested, based on UV-visible and EPR spectroscopy, that the ribonucleotide reductase from Corynebac-terium ammoniagenes contains Mn rather than Fe in its native form. However, more recent crystallographic studies have shown that this protein is structurally identical to the native iron proteins and apparently does not contain a Mn active... 

The electronic structure of several model complexes for mononuclear iron proteins has been evaluated by gas-phase photodetachment photoelectron spectroscopy. Molecules of interest are negatively charged, such as Fe(SCN)3, Fe(SCN)4, and Fe(SCN)4. The anions were transported into the gas phase by electrospray ionization isolated Fe(SCN)4 was not detected in the gas phase, but rather was trapped as the stabilized ion pair Na+ [Fe(SCN)4 ]. 

Averill, B., and Vincent, JB (1993). Electronic absorption spectroscopy of nonheme iron proteins. 

Mossbauer spectroscopy of Fe-enriched MoFe protein in dithionite-reduced and dye-oxidized oxidation states were interpreted in terms of approximately 50% of the Fe in the protein being present in cubane clusters similar to [4Fe-4S] clusters of simpler Fe-S proteins, e.g., ferredoxins and Chromatium high-potential iron proteins. Spectra of MoFe protein in which P clusters were selectively enriched with Fe were consistent with two of the clusters having slightly different environments. 

This feature of the process may be clarified by the use of spectroscopic methods. EPR (28), EXAFS 115), and Mbssbauer 12,155) spectroscopies have been applied to the study of the early stages of iron uptake and core formation and various types of iron clusters have been identified. For example, Chasteen et al. 28) have shown by EPR that a spin-coupled Fe -Fe dimer is produced at low iron protein ratios. Allied to the mutagenesis-crystallographic approach, spectroscopic examinations should aid the identification of ferroxidase and nuclea-tion sites. 

Mineeva RM (1978) Relationship between Mdssbauer spectra and defect structure in biotites from electric field gradient calculations. Phys Chem Minerals 2 267-277 Mizutani T, Fukushima Y, Kobayashi T (1991) Synthesis of 1 1 and 2 1 iron phyllosihcates and characterization of their iron state by Mdssbauer spectroscopy. Clays Clay Minerals 39 381-386 Moon N, Coffin CT, Steinke DC, Sands RH, Dnnham WR (1996) A high-sensitivity Mdssbaner spectrometer facilitates the study of iron proteins at natural abundance. Nncl Instr Meth Phys Res B 119 555-564... 

Fluorine-labeled analogues of C. vinosum high-potential iron protein have been investigated by F NMR spectroscopy. By incorporation of specific fluorine-labeled amino acid residues, one can insert unique probes at well-defined locations within the protein core. The synthesis and purification of 2-, 3-, and 4-fluorophenylalanine (abbreviated 2-F-, 3-F-, and 4-F-Phe, respectively), 3-fluorotyrosine (3-F-Tyr), and 5-fluorotr3q)tophan (5-F-Trp) derivatives of C. vinosum HiPIP, the assignment of F NMR resonances, the measurement of longitudinal relaxation times, and the temperature dependence of F and resonances have all been reported 42, 43, 136). These measurements were used to examine structural perturbations of mutants, the dynamics of interaction of residues with the cluster, and solvent accessibility, and as a test of the relative contribution of cross-relaxation to magnetization decay. 

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