Signal-to-noise ratio (SNR), RF field (B 1 ), and RF power requirement for human head imaging were examined at 7T and 4T magnetic field strengths. The variation in B 1 magnitude was nearly twofold higher at 7T than at 4T (ϳ42% compared to ϳ23%). The power required for a 90°pulse in the center of the head at 7T was approximately twice that at 4T. The SNR averaged over the brain was at least 1.6 times higher at 7T compared to 4T. These experimental results were consistent with calculations performed using a human head model and Max In the last decade, MRI studies conducted at 4T have demonstrated the utility of high magnetic fields in functional and anatomical imaging of the human brain and for spectroscopy studies in the brain and the human body (1-7). These accomplishments and the continued successes at magnetic fields up to 9.4T with animal models have paved the way for the exploration of magnetic fields of higher than 4T for human brain studies (8 -12). Consequently, recent efforts have been undertaken to establish 8T and 7T systems, the latter in our laboratory (13)(14)(15). Now with an operational 7T system, the signal-to-noise ratio (SNR), RF field (B 1 ), and RF power requirement at 7T were compared to the same parameters at 4T. MATERIALS AND METHODSIn this 7T vs. 4T comparison study, we used the same size coils, the same model consoles, identical acquisition parameters, and the same volunteers for six carefully reproduced experiments at each field strength. Hardware SystemsThis experiment was performed on Varian Unity Inova consoles interfaced to 90 cm bore Oxford 4T and Magnex 7T magnets. The noise figures of the two systems were the same, measuring 1.3 dB. Siemens body gradients (65 cm i.d.) and Magnex head gradients (38 cm i.d.) were used in the 4T and 7T systems, respectively. Coils

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The chemical identity of the amino acid free-radical site that represents one of the two oxidizing equivalents stored in the H2O2-oxidized intermediate (compound ES) of the mitochondrial heme enzyme, cytochrome c peroxidase (CcP) has been sought for almost a quarter of a century. Site-directed mutagenesis alone cannot yield this answer. Low-temperature 35-gigahertz (Q-band) electron nuclear double resonance (ENDOR) spectroscopy was used to examine compound ES prepared from proteins containing specifically deuterated methionine or tryptophan, as well as the amino acid replacement Trp51----Phe. The results definitely identify the site of the radical in compound ES as tryptophan, most likely Trp191.