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Abstract-Transmission switching (TS) has shown to be an effective power flow control tool. TS can reduce the system cost, improve system reliability, and enhance the management of intermittent renewable resources. This paper addresses the state of the art problem of TS by developing an AC-based real-time contingency analysis (RTCA) package with TS. The package is tested on real power system data, taken from energy management systems of PJM, TVA, and ERCOT. The results show that postcontingency corrective switching is a ready to be implemented transformational technology that provides substantial reliability gains. The computational time and the performance of the developed RTCA package, reported in the paper, are promising.

The kinetics of electron transfer of cytochrome c2 from Rhodobacter sphaeroides, Rhodobacter capsulatus, and Rhodospirillum centenum to reaction centers from Rb. sphaeroides and Rb. capsulatus have been measured. Observed in the kinetics of decay of the oxidized donor are a rapid first-order rate and one or more slower rates that are due to diffusion-limited complex formation. For reaction centers from Rb. sphaeroides, the fast component had time constants of 1.0 and 0.5 microsecond for cytochrome c2 from Rb. sphaeroides and Rb. capsulatus, respectively, but only a slow component was observed for cytochrome c2 from Rs. centenum. For reaction centers from Rb. capsulatus, the kinetics from all three cytochromes had a fast component with time constants of 1.0, 0.7, and 1.9 microseconds for cytochrome c2 from Rb. sphaeroides, Rb. capsulatus, and Rs. centenum, respectively, although the dissociation constant for cytochrome c2 from Rs. centenum was approximately 20 times larger than that of the other cytochromes. The observation of the fast component for cytochrome c2 from Rs. centenum in reaction centers from Rb. capsulatus but not Rb. sphaeroides demonstrates that the binding interactions for the two reaction centers differ, and the involvement of amino acid residues in the binding is discussed. The kinetics of electron transfer from cytochrome c2 to reaction centers of Rb. sphaeroides from wild type and three mutant strains that have altered carboxyl-terminal regions of the M subunit of the reaction center have also been measured. For cytochrome c2 from Rb. sphaeroides, the kinetics are very similar between the mutants and wild type.(ABSTRACT TRUNCATED AT 250 WORDS)

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