Chlamydial ribonucleotide reductase: Tyrosyl radical function in catalysis replaced by the FeIII-FIV cluster.

Ribonucleotide reductase (RNR) from Chlamydia trachomatis is a class I RNR composed of proteins R1 and R2. In protein R2, the tyrosine residue harboring the radical that is necessary for catalysis in other class I RNRs is replaced by a phenylalanine. Active C. trachomatis RNR instead uses the Fe^III–Fe^IV state of the iron cluster in R2 as an initiator of catalysis. The paramagnetic Fe^III–Fe^IV state, identified by ⁵⁷Fe substitution, becomes electron spin resonance detectable in samples that are frozen during conditions of ongoing catalysis. Its amount depends on the conditions for catalysis, such as incubation temperature and the R1/R2 ratio. The results link induction of the Fe^III–Fe^IV state with enzyme activity of chlamydial RNR. Based on these observations, a reaction scheme is proposed for the iron site. This scheme includes (i) an activation cycle involving reduction and an oxygen reaction in R2 and (ii) a catalysis cycle involving substrate binding and turnover in R1. [ABSTRACT FROM AUTHOR]