Journal
JOURNAL OF BIOLOGICAL INORGANIC CHEMISTRY
Volume 21, Issue 1, Pages 39-52Publisher
SPRINGER
DOI: 10.1007/s00775-015-1329-4
Keywords
Flavodiiron; Diiron; Oxygen; Nitric oxide; Reactive oxygen species
Funding
- Portuguese Fundacao para a Ciencia e Tecnologia (FCT)
- FCT [SFRH/BPD/94050/2013, SFRH/BD/85106/2012]
- FCT MosMicro Unit [UID/CBQ/04612/2013]
- iNOVA4Health [UID/Multi/04462/2013]
- FCT/Ministerio da Educacao e Ciencia
- FEDER under the PT2020 Partnership Agreement
- Fundação para a Ciência e a Tecnologia [SFRH/BD/85106/2012] Funding Source: FCT
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Flavodiiron proteins have emerged in the last two decades as a newly discovered family of oxygen and/or nitric oxide reductases widespread in the three life domains, and present in both aerobic and anaerobic organisms. Herein we present the main features of these fascinating enzymes, with a particular emphasis on the metal sites, as more appropriate for this special issue in memory of the exceptional bioinorganic scientist R. J. P. Williams who pioneered the notion of (metal) element availability-driven evolution. We also compare the flavodiiron proteins with the other oxygen and nitric oxide reductases known until now, highlighting how throughout evolution Nature arrived at different solutions for similar functions, in some cases adding extra features, such as energy conservation. These enzymes are an example of the (bioinorganic) unpredictable diversity of the living world.
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