scholarly journals Selenocysteine Substitution in a Class I Ribonucleotide Reductase

Biochemistry ◽  
2019 ◽  
Vol 58 (50) ◽  
pp. 5074-5084 ◽  
Author(s):  
Brandon L. Greene ◽  
JoAnne Stubbe ◽  
Daniel G. Nocera
Keyword(s):  
Ribonucleotide Reductase ◽  
Class I

Peroxo-Type Intermediates in Class I Ribonucleotide Reductase and Related Binuclear Non-Heme Iron Enzymes

2009 ◽  
Vol 131 (34) ◽  
pp. 12155-12171 ◽  
Author(s):  
Kasper P. Jensen ◽  
Caleb B. Bell, ◽  
Michael D. Clay ◽  
Edward I. Solomon
Keyword(s):  
Ribonucleotide Reductase ◽  
Heme Iron ◽  
Class I ◽  
Non Heme Iron ◽  
Iron Enzymes

scholarly journals Structural Basis for Superoxide Activation of Flavobacterium johnsoniae Class I Ribonucleotide Reductase and for Radical Initiation by Its Dimanganese Cofactor

Biochemistry ◽  
2018 ◽  
Vol 57 (18) ◽  
pp. 2679-2693 ◽  
Author(s):  
Hannah R. Rose ◽  
Manas K. Ghosh ◽  
Ailiena O. Maggiolo ◽  
Christopher J. Pollock ◽  
Elizabeth J. Blaesi ◽  
...  
Keyword(s):  
Ribonucleotide Reductase ◽  
Class I ◽  
Structural Basis ◽  
Radical Initiation ◽  
Flavobacterium Johnsoniae

scholarly journals Direct Measurement of the Radical Translocation Distance in the Class I Ribonucleotide Reductase fromChlamydia trachomatis

2015 ◽  
Vol 119 (43) ◽  
pp. 13777-13784 ◽  
Author(s):  
Jovan Livada ◽  
Ryan J. Martinie ◽  
Laura M. K. Dassama ◽  
Carsten Krebs ◽  
J. Martin Bollinger ◽  
...  
Keyword(s):  
Direct Measurement ◽  
Ribonucleotide Reductase ◽  
Class I

scholarly journals The Conserved Active Site Asparagine in Class I Ribonucleotide Reductase Is Essential for Catalysis

2001 ◽  
Vol 277 (8) ◽  
pp. 5749-5755 ◽  
Author(s):  
Alex Kasrayan ◽  
Annika L. Persson ◽  
Margareta Sahlin ◽  
Britt-Marie Sjöberg
Keyword(s):  
Ribonucleotide Reductase ◽  
Active Site ◽  
Class I

Radical Initiation in the Class I Ribonucleotide Reductase: Long-Range Proton-Coupled Electron Transfer?

ChemInform ◽  
2003 ◽  
Vol 34 (32) ◽  
Author(s):  
JoAnne Stubbe ◽  
Daniel G. Nocera ◽  
Cyril S. Yee ◽  
Michelle C. Y. Chang
Keyword(s):  
Electron Transfer ◽  
Long Range ◽  
Ribonucleotide Reductase ◽  
Class I ◽  
Radical Initiation ◽  
Proton Coupled Electron Transfer

scholarly journals Metal-free class Ie ribonucleotide reductase from pathogens initiates catalysis with a tyrosine-derived dihydroxyphenylalanine radical

2018 ◽  
Vol 115 (40) ◽  
pp. 10022-10027 ◽  
Author(s):  
Elizabeth J. Blaesi ◽  
Gavin M. Palowitch ◽  
Kai Hu ◽  
Amelia J. Kim ◽  
Hannah R. Rose ◽  
...  
Keyword(s):  
Ribonucleotide Reductase ◽  
Metal Ion ◽  
Pathogenic Bacteria ◽  
Cysteine Residue ◽  
Class I ◽  
Tyrosyl Radical ◽  
Human Pathogens ◽  
Α Subunit ◽  
Metal Free ◽  
Iron Deprivation

All cells obtain 2′-deoxyribonucleotides for DNA synthesis through the activity of a ribonucleotide reductase (RNR). The class I RNRs found in humans and pathogenic bacteria differ in (i) use of Fe(II), Mn(II), or both for activation of the dinuclear-metallocofactor subunit, β; (ii) reaction of the reduced dimetal center with dioxygen or superoxide for this activation; (iii) requirement (or lack thereof) for a flavoprotein activase, NrdI, to provide the superoxide from O2; and (iv) use of either a stable tyrosyl radical or a high-valent dimetal cluster to initiate each turnover by oxidizing a cysteine residue in the α subunit to a radical (Cys•). The use of manganese by bacterial class I, subclass b-d RNRs, which contrasts with the exclusive use of iron by the eukaryotic Ia enzymes, appears to be a countermeasure of certain pathogens against iron deprivation imposed by their hosts. Here, we report a metal-free type of class I RNR (subclass e) from two human pathogens. The Cys• in its α subunit is generated by a stable, tyrosine-derived dihydroxyphenylalanine radical (DOPA•) in β. The three-electron oxidation producing DOPA• occurs inEscherichia colionly if the β is coexpressed with the NrdI activase encoded adjacently in the pathogen genome. The independence of this new RNR from transition metals, or the requirement for a single metal ion only transiently for activation, may afford the pathogens an even more potent countermeasure against transition metal-directed innate immunity.

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