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PubMed1987

Conformational change accompanies redox reactions of the tetraheme cytochrome c-554 of Nitrosomonas europaea.

Cytochrome c-554 of the ammonia-oxidizing chemolithoautotropic bacteria is thought to mediate electron transfer from hydroxylamine oxidoreductase to a terminal oxidase and/or to ammonia monooxygenase. The cytochrome has four c hemes which interact magnetically and have the same redox potential. We report that the kinetics of reduction of ferric cytochrome c-554 by dithionite or the oxidation of ferrous cytochrome c-554 by O2 or H2O2 are complex and multiphasic. Transient rapid-scan difference spectra indicate discrete maxima at approximately 418 nm, 425 nm and 432 nm. Absorbance changes at all three difference maxima appear to occur in all kinetic phases, although not in equal amounts for each wavelength. Reduction by 20 mM dithionite was biphasic. At pH 7.5 the first phase, which involved approximately 50% of the total absorbance change, had a rate constant (20 degrees C) of 140 s-1 and energy of activation of 20 kJ X mol-1. The slow phase had a rate constant 0.43 s-1 and a relatively high energy of activation, 87 kJ X mol-1, suggesting that a change in protein configuration accompanied the reaction. As the pH of the solution increased, the rate constant for both phases decreased and the fraction of absorbance change in the rapid phase increased. Oxidation of ferrous cytochrome c-554 by O2 involved a discrete rapid phase with a rate constant of 14 s-1, accounting for 6% of the absorbance. The remainder of the reaction was multiphasic with rate constants in the range 0.1-0.01 s-1. With H2O2 as the oxidant, the rapid phase involved 39% of the change in absorbance with a rate constant of 19 s-1. The remainder of the reoxidation was multiphasic with rate constants ranging over 0.4-0.01 s-1.

Cytochrome c Group↗
PubMed1967

Uptake and utilization of amino acids by resting cells of Nitrosomonas europaea.

Incorporation of selected amino acids by resting cells was studied with regard to effects of concentration, rate and extent of incorporation, cellular distribution, effect of ammonium ion on uptake, and competitive effects. l-Aspartic acid, l-alanine, l-serine, and glycine presented at trace levels were incorporated at rates ranging from 0.11 to 8.2 mumumoles per mg (dry weight) per minute, and maximal incorporation was 11 to 333 mumumoles per mg (dry weight). When glycine and aspartic acid were supplied at substrate level, the rate of incorporation increased 14- and 109-fold, respectively. The presence of ammonium ion further increased both the rate and extent of uptake of glycine and aspartic acid. The distribution of cellular radioactivity arising from (14)C amino acids indicated that cell pool radioactivity was concentrated from 1.2- to 24.5-fold over the external medium. Aspartic acid pool radioactivity accounted for 50% or more of the total cellular radioactivity, whereas radioactivity in glycine and serine pools dropped from initially high levels to 20 to 25% during incubation. The decrease in pool radioactivity with both glycine and serine was accompanied by an increase in other fractions, especially in the cell residue. The growth-inhibiting amino acid l-valine, supplied at substrate level, contributed more carbon per milligram (dry weight) than any other amino acid studied. l-Leucine, in the presence of l-valine, was observed to decrease valine incorporation.

Amino Acids↗