A designed heme-[4Fe-4S] metalloenzyme catalyzes sulfite reduction like the native enzyme
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چکیده
منابع مشابه
Proton coupling to [4Fe-4S](2+/+) and [4Fe-4Se](2+/+) oxidation and reduction in a designed protein.
The coupling of a single proton to [4Fe-4S]2+/+ oxidation/reduction in a de novo designed iron-sulfur protein maquette is presented. The reduced state pKared is 9.3, and the oxidized state pKaox is <6.5. The reduced state pKared shifts to 8.3 upon incorporation of a [4Fe-4Se]2+/+ cluster, implicating the cluster itself or its primary coordination sphere as the proton-coupling site.
متن کاملA Designed Metalloenzyme Achieving the Catalytic Rate of a Native Enzyme
Terminal oxidases catalyze four-electron reduction of oxygen to water, and the energy harvested is utilized to drive the synthesis of adenosine triphosphate. While much effort has been made to design a catalyst mimicking the function of terminal oxidases, most biomimetic catalysts have much lower activity than native oxidases. Herein we report a designed oxidase in myoglobin with an O2 reductio...
متن کاملHigh and low reduction potential 4Fe-4S clusters in Azotobacter vinelandii (4Fe-4S) 2ferredoxin I. Influence of the polypeptide on the reduction potentials.
Azotobacter vinelandii (4Fe-4S)2 ferredoxin I (Fd I) is an electron transfer protein with Mr equals 14,500 and Eo equals -420 mv. It exhibits and EPR signal of g equals 2.01 in its isolated form. This resonance is almost identical with the signal that originates from a "super-oxidized" state of the 4Fe-4S cluster of potassium ferricyanide-treated Clostridium ferredoxin. A cluster that exhibits ...
متن کاملSequential oxidation of the cubane [4Fe--4S] cluster from [4Fe--4S](-) to [4Fe--4S](3+) in Fe(4)S(4)L(n)(-) complexes.
Gaseous Fe(4)S(n)(-) (n = 4-6) clusters and synthetic analogue complexes, Fe(4)S(4)L(n)(-) (L = Cl, Br, I; n = 1-4), were produced by laser vaporization of a solid Fe/S target and electrospray from solution samples, respectively, and their electronic structures were probed by photoelectron spectroscopy. Low binding energy features derived from minority-spin Fe 3d electrons were clearly distingu...
متن کاملStructure of the dissimilatory sulfite reductase from the hyperthermophilic archaeon Archaeoglobus fulgidus.
Conservation of energy based on the reduction of sulfate is of fundamental importance for the biogeochemical sulfur cycle. A key enzyme of this ancient anaerobic process is the dissimilatory sulfite reductase (dSir), which catalyzes the six-electron reduction of sulfite to hydrogen sulfide under participation of a unique magnetically coupled siroheme-[4Fe-4S] center. We determined the crystal s...
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ژورنال
عنوان ژورنال: Science
سال: 2018
ISSN: 0036-8075,1095-9203
DOI: 10.1126/science.aat8474