In this review we have focused much of our discussion on the mechanistic details of how the native enzymes function and how mechanistic developments/insights with synthetic small molecule complexes possessing SOD activity have influenced our understanding of the electron transfer processes involved with the natural enzymes. A few overriding themes have emerged. Clearly, the SOD enzymes operate at near diffusion controlled rates and to achieve such catalytic turnover activity, several important physical principles must be operative. Such fast electron transfer processes requires a role for protons; i.e., proton-coupled electron transfer (''H-atom transfer'') solves the dilemma of charge separation developing in the transition state for the electron transfer step. Additionally, outer-sphere electron transfer is likely a most important pathway for manganese and iron dismutases. This situation arises because the ligand exchange rates on these two ions in water never exceed {approx}10{sup +7} s{sup -1}; consequently, 10{sup +9} catalytic rates require more subtle mechanistic insights. In contrast, copper complexes can achieve diffusion controlled (>10{sup +9}) exchange rates in water; thus inner-sphere electron transfer processes are more likely to be operative in the Cu/Zn enzymes. Recent studies have continued to expand our understanding of the mechanism of action of this most important class …

Interview with William Coffey, a Navy WWII veteran from Hopkins County, Texas. Coffey discusses joining the Navy in 1937, boot camp in San Diego, service aboard the USS Oklahoma (BB-37), transfer to submarines in the Philippines, the bombing of Cavite Navy Yard at the start of the war, assignment to the S-41 as a cook, combat around the Solomon Islands, attaining submarine qualifications, patrolling the northern Pacific, the character of the crew, transfer to the USS Sterlet (SS-392), patrols, medical leave, and service postwar.