Cruise 5 of the N. B. Scofield for 1954. Cruise Report 54-S-5

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Cruise 2 of the N.B. Scofield for 1955. Cruise Report 55-S-2

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Cruise 3 of the N.B. Scofield for 1955. Cruise Report 55-S-3

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Cruise 4 of the N.B. Scofield for 1955. Cruise Report 55-S-4

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Cruise 56-B-1 of the N.B. Scofield April 26 to 4 June 1956. Cruise Report 56-S-2

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Cruise three of the N.B. Scofield for 1956. Cruise Report 56-S-3

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Cruise four of the N.B. Scofield for 1956. Cruise Report 56-S-4

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Cruise 5 of the N.B. Scofield for 1956. Cruise Report 56-S-5

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Cruise 6 of the N.B. Scofield for 1956. Cruise Report 56-S-6

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Cruise 7 of the N.B. Scofield for 1956. Cruise Report 56-S-7

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Cruise 8 of the N.B. Scofield for 1956. Cruise Report 56-S-8

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Cruise 57-S-1 of the N.B. Scofield

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Cruise 3 of the N.B. Scofield for 1957.

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Cruise 5 of the N.B. Scofield for 1957.

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Preparation, characterization and intramolecular electron-transfer studies of ruthenium-modified cytochromes c

Redox-active ruthenium complexes have been covalently attached to the surface of a series of natural, semisynthetic and recombinant cytochromes c. The protein derivatives were characterized by a variety of spectroscopic techniques. Distant Fe^(2+) - Ru^(3+) electronic couplings were extracted from intramolecular electron-transfer rates in Ru(bpy)_2(im)HisX (where X= 33, 39, 62, and 72) derivatives of cyt c. The couplings increase according to 62 (0.0060) < 72 (0.057) < 33 (0.097) < 39 (0.11 cm^(-1)); however, this order is incongruent with histidine to heme edge-edge distances [62 (14.8) > 39 (12.3) > 33 (11.1) > =72 (8.4 Å)]. These results suggest the chemical nature of the intervening medium needs to be considered for a more precise evaluation of couplings. The rates (and couplings) correlate with the lengths of a-tunneling pathways comprised of covalent bonds, hydrogen bonds and through-space jumps from the histidines to the heme group. Space jumps greatly decrease couplings: one from Pro71 to Met80 extends the σ-tunneling length of the His72 pathway by roughly 10 covalent bond units. Experimental couplings also correlate well with those calculated using extended Hiickel theory to evaluate the contribution of the intervening protein medium.

Two horse heart cyt c variants incorporating the unnatural amino acids (S)-2- amino-3-(2,2'-bipyrid-6-yl)-propanoic acid (6Bpa) and (S)-2-amino-3-(2,2'-bipyrid-4-yl)propanoic acid ( 4Bpa) at position 72 have been prepared using semisynthetic protocols. Negligible perturbation of the protein structure results from this introduction of unnatural amino acids. Redox-active Ru(2,2'-bipyridine)_2^(2+) binds to 4Bpa72 cyt c but not to the 6Bpa protein. Enhanced ET rates were observed in the Ru(bpy)_2^(2+)-modified 4Bpa72 cyt c relative to the analogous His72 derivative. The rapid (< 60 nanosecond) photogeneration of ferrous Ru-modified 4Bpa72 cyt c in the conformationally altered alkaline state demonstrates that laser-induced ET can be employed to study submicrosecond protein-folding events.