Forward and reverse electron transfer with the Y356DOPA-β2 heterodimer of E. coli ribonucleotide reductase

Journal of the American Chemical Society

Volumn 129, Issue 8, 2007, Pages 2226-2227

  Seyedsayamdost, Mohammad R ^a   Stubbe, JoAnne ^a  

^a MASSACHUSETTS INSTITUTE OF TECHNOLOGY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

DOPA; RIBONUCLEOTIDE REDUCTASE; YTTRIUM;

ALLOSTERISM; ARTICLE; CARBOXY TERMINAL SEQUENCE; CHEMICAL REACTION KINETICS; CONFORMATION; ELECTRON TRANSPORT; ENZYME MECHANISM; ESCHERICHIA COLI; NONHUMAN; NUCLEOTIDE SEQUENCE; STEADY STATE;

AMINO ACID SUBSTITUTION; CATALYSIS; DIHYDROXYPHENYLALANINE; ELECTRONS; ESCHERICHIA COLI; FREE RADICALS; KINETICS; OXIDATION-REDUCTION; RIBONUCLEOTIDE REDUCTASES; TIME FACTORS;

EID: 33847666363     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja0685607     Document Type: Article

References (18)

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11. d of 13 μM was determined for the interaction of α2 with ββ′, where the β′ monomer was missing the last 30 residues.
12. 14C]-CDP was 8150 cpm/nmol.
13. -1, which can be accommodated by the mechanism proposed in Figure 3.
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15. 122•; decay or DOPA•; formation is observed by SF or EPR spectroscopies (see Figure S5).
16. 3NDP (ref 14) as well as with DOPA-β2 (ref 6) have suggested an asymmetry in the α2/β2 interaction. With DOPA-ββ′, additional asymmetry is provided by removal of the last 22 residues in the β′-monomer. A model to account for differences in the yield of DOPA•; between DOPA-β2 and DOPA-ββ′ will be described in detail elsewhere (manuscript in preparation).
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18. c.