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Roles of key active-site residues in flavocytochrome P450 BM3.
TLDR
Mutants F87G and F87Y not only exhibit increased Km and decreased kcat values for fatty acid oxidation, but also undergo an irreversible conversion process from a 'fast' to a 'slow' rate of substrate turnover. Expand
P450 BM3: the very model of a modern flavocytochrome.
TLDR
The fundamental properties of P 450 BM3 are discussed and how progress with this model P450 has affected the authors' comprehension of P450 systems in general is discussed. Expand
Interaction of the Escherichia coli replication terminator protein (Tus) with DNA: a model derived from DNA-binding studies of mutant proteins by surface plasmon resonance.
TLDR
The kinetic and thermodynamic data suggest a model for Tus binding to TerB which involves an ordered series of events that include structural changes in the protein. Expand
Rational re‐design of the substrate binding site of flavocytochrome P450 BM3
TLDR
Removing the arginine 47/lysine 51 carboxylate binding motif at the mouth of the active site disfavours binding of all fatty acids, indicating its importance in the initial recognition of substrates. Expand
Oxygen activation and electron transfer in flavocytochrome P450 BM3.
TLDR
Kinetic analysis of the mutants indicated that the spin-state shift alone accelerates the rate of heme reduction by 200-fold and that the concomitant shift in reduction potential is only responsible for a modest 2-fold rate enhancement. Expand
NMR structure of the N-terminal domain of E. coli DnaB helicase: implications for structure rearrangements in the helicase hexamer.
TLDR
The monomer-dimer equilibrium observed for the N-terminal domain of DnaB is likely to be of functional significance for helicase activity, by participating in the switch between C6 and C3 symmetry of the helicase hexamer. Expand
Three-dimensional reconstructions from cryoelectron microscopy images reveal an intimate complex between helicase DnaB and its loading partner DnaC.
TLDR
The structures of the DnaB helicase hexamer and its complex with DnaC reveal some interesting structural features relevant to helicase function and to the assembly of the two-protein complex, the first report of a three-dimensional structure of a helicase obtained using cryoelectron microscopy. Expand
A Proton Delivery Pathway in the Soluble Fumarate Reductase from Shewanella frigidimarina*
TLDR
Fast scan protein-film voltammetric studies on wild-type and R381K enzymes show that the proton transfer pathway delivers one proton per catalytic cycle and is not required for transporting the other proton, which transfers as a hydride from the reduced, protonated FAD. Expand
Catalysis in fumarate reductase.
TLDR
The structures of fumarate reductases from two Shewanella species have been determined and it is suggested that this function is provided by an arginine side chain, confirmed experimentally by analysing the effects of site-directed mutations on enzyme activity. Expand
Phenylalanine 393 exerts thermodynamic control over the heme of flavocytochrome P450 BM3.
TLDR
It is postulate that the nature of the residue at position 393 is important in controlling the delicate equilibrium observed in P450s, whereby a tradeoff is established between the rate of heme reduction and the rate at which the ferrous heme can bind and, subsequently, reduce molecular oxygen. Expand
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