Myoglobin transfer

Ortiz de Montellano PR, Catalano CE (1985) Epoxidation of styrene by haemoglobin and myoglobin. Transfer of oxygen equivalents to the protein surface. J Biol Chem 260 9265-9271... 

Biosensors based on direct electron transfer of myoglobin... 

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A.E.F. Nassar, Z. Zhang, N.F. Hu, J.F. Rusling, and T. Kumosinski, Protein-coupled electron transfer from electrodes to myoglobin in ordered biomembrane-like films. J. Phys. Chem. B 101, 2224-2231 (1997). 

Figure 2.9. Schematic of a matrix-assisted laser desorption/ionization (MALDI) event. The SEM micrograph depicts sinapinic acid-equine myoglobin crystal from a sample prepared according to the dried drop sample preparation method. In the desorption event neutral matrix molecules (M), positive matrix ions (M+), negative matrix ions (M-), neutral analyte molecules (N), positive analyte ions (+), and negative analyte ions (-) are created and/or transferred to the gas phase. Reprinted from A. Westman-Brinkmalm and G. Brinkmalm (2002). In Mass Spectrometry and Hyphenated Techniques in Neuropeptide Research, J. Silberring and R. Ekman (eds.) New York John Wiley Sons, 47-105. With permission of John Wiley Sons, Inc.

Fig. 8. A view into the interior of a ruthenium modified myoglobin where the amino acids in the vicinity of Trp-14 are shown. The dots correspond to the statistieal density Pn i,(r) of (discretized) tunneling path vertices (rj in Eq. 26) from 500,000 tunneling paths [19], The (r) is clustered in a cylindrical zone centered on the average path, shown as the light line appearing in the center and emerging toward the viewer. The computation modeled paths of electron transfer in Ru(His-12) myoglobin studied experimentally by Gray and coworkers [88]...

Electron transfer to the protein metal center is monitored spectroscopically. In the case of a heme (FeP), a fast increase in absorbance due to direct reduction of Fe(III)P by Ru(bpy)f is followed by a slower increase in absorbance due to reduction of Fe(III)P by the Ru(II) on the protein surface. Control flash experiments with unmodified proteins show only the fast initial increase in absorbance due to Fe(III)P reduction by Ru(bpy)3. Such control experiments demonstrate for horse heart cytochrome c [21], azurin [28], and sperm whale myoglobin [14] that slow reduction of the heme by the EDTA radical produced in the scavenging step does not occur in competition with intramolecular ET. However, for Candida krusei cytochrome c, the control experiment shows evidence for slow EDTA radical reduction of the heme after initial fast reduetion by Ru(bpy)i+ [19]. 

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