High Potential Iron Sulfur Proteins

Carter, Charles W.

doi:10.1002/0470028637.met143

Cited by 2 publications

(3 citation statements)

References 43 publications

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“…For example. there are reports of FeS clusters that are significantly more buried than their counterparts, but no significant redox potential difference is observed between them [162]. …”

Section: Discussionmentioning

confidence: 99%

“…The transitions that a metal center can go through are a major determinant of the overall range of E° for a metalloprotein. The main reason for the higher reduction potentials observed in the [4Fe-4S] clusters in high potential iron-sulfur proteins (HiPIPs) compared with those in ferredoxins (100–500 mV vs. −600–100 mV, respectively) [10] is the different transitions they go through ([4Fe-4S] 2+/3+ vs. [4Fe-4S] 1+/2+ , respectively) [159–162]. …”

Section: Factors Affecting Redox Potentials Of Et Centers and Stramentioning

confidence: 99%

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Design and fine-tuning redox potentials of metalloproteins involved in electron transfer in bioenergetics

Hosseinzadeh¹,

Lu²

2016

Biochimica et Biophysica Acta (BBA) - Bioenergetics

163

121

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Redox potentials are the major contributors to controlling the ET rates and thus regulating ET processes in the bioenergetics. To maximize the efficiency of the ET process, one needs to master the art of tuning of the E°, especially metalloproteins, as they represent major classes of ET proteins. In this review, we first describe the importance of tuning E° of ET centers, including the metalloproteins described above, and its role in regulating the ET in bioenergetic processes including photosynthesis and respiration. The major focus of this review is to summarize recent work in designing the ET centers, namely cupredoxins, cytochromes, and iron-sulfur proteins, and examples in design of protein networks involved these ET centers. We then discuss the factors that affect redox potentials of these ET centers including metal ion, the ligands to metal center and interactions beyond the primary ligand, especially non-covalent secondary coordination sphere interactions. We gave examples of strategies to fine-tune the redox potential using both natural and unnatural amino acids and native and nonnative cofactors. Several case studies are used to illustrate recent successes in this area. Outlooks for future endeavors are also provided.

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“…For example. there are reports of FeS clusters that are significantly more buried than their counterparts, but no significant redox potential difference is observed between them [162]. …”

Section: Discussionmentioning

confidence: 99%

Section: Factors Affecting Redox Potentials Of Et Centers and Stramentioning

confidence: 99%

Design and fine-tuning redox potentials of metalloproteins involved in electron transfer in bioenergetics

Hosseinzadeh¹,

Lu²

2016

Biochimica et Biophysica Acta (BBA) - Bioenergetics

163

121

View full text Add to dashboard Cite

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“…The motivation to develop alternative energy sources that are clean, abundant and renewable has directed great attention to understanding the science and mimicking the function of natural photosynthesis. − Natural photosynthesis has converted solar energy to stored chemical energy to maintain the diversity of living organisms for more than 3 billion years. − An intense research effort is focused on simplifying natural photosynthesis while integrating the core reaction centers in a common structural system to achieve similar results to those found in nature. − For example, the chemistry of cubane Fe 4 S 4 clusters, which are ubiquitous in nature, has developed into a mature research area with various analogous inorganic and organometallic molecules. − In nature, Fe 4 S 4 clusters are involved in redox processes such as photosynthesis, nitrogen fixation, and respiration, and frequently found in both electron pathways and in active sites of metalloenzymes. ,,− They are electron carriers in some enzymes such as ferredoxin, hydrogenase, and nitrogenase, and compose active sites in others including sulfite reductase, [FeFe] hydrogenase, and acetyl coenzyme A synthase. ,− In natural enzymes, the active Fe 4 S 4 clusters are often coordinated in highly evolved systems with complex biochemical pathways to perform their catalytic and electron-transferring functions. ,,, …”

Section: Introductionmentioning

confidence: 99%

Tunable Biomimetic Chalcogels with Fe₄S₄ Cores and [Sn_nS_2n+2]^4–(n = 1, 2, 4) Building Blocks for Solar Fuel Catalysis

et al. 2013

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Biology sustains itself by converting solar energy in a series of reactions between light harvesting components, electron transfer pathways, and redox-active centers. As an artificial system mimicking such solar energy conversion, porous chalcogenide aerogels (chalcogels) encompass the above components into a common architecture. We present here the ability to tune the redox properties of chalcogel frameworks containing biological Fe(4)S(4) clusters. We have investigated the effects of [Sn(n)S(2n+2)](4-) linking blocks ([SnS(4)](4-), [Sn(2)S(6)](4-), [Sn(4)S(10)](4-)) on the electrochemical and electrocatalytic properties of the chalcogels, as well as on the photophysical properties of incorporated light-harvesting dyes, tris(2,2'-bipyridyl)ruthenium(II) (Ru(bpy)(3)(2+)). The various thiostannate linking blocks do not alter significantly the chalcogel surface area (90-310 m(2)/g) or the local environment around the Fe(4)S(4) clusters as indicated by (57)Fe Mössbauer spectroscopy. However, the varying charge density of the linking blocks greatly affects the reduction potential of the Fe(4)S(4) cluster and the electronic interaction between the clusters. We find that when the Fe(4)S(4) clusters are bridged with the adamantane [Sn(4)S(10)](4-) linking blocks, the electrochemical reduction of CS(2) and the photochemical production of hydrogen are enhanced. The ability to tune the redox properties of biomimetic chalcogels presents a novel avenue to control the function of multifunctional chalcogels for a wide range of electrochemical or photochemical processes relevant to solar fuels.

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High Potential Iron Sulfur Proteins

Cited by 2 publications

References 43 publications

Design and fine-tuning redox potentials of metalloproteins involved in electron transfer in bioenergetics

Design and fine-tuning redox potentials of metalloproteins involved in electron transfer in bioenergetics

Tunable Biomimetic Chalcogels with Fe₄S₄ Cores and [Sn_nS_2n+2]^4–(n = 1, 2, 4) Building Blocks for Solar Fuel Catalysis

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High Potential Iron Sulfur Proteins

Cited by 2 publications

References 43 publications

Design and fine-tuning redox potentials of metalloproteins involved in electron transfer in bioenergetics

Design and fine-tuning redox potentials of metalloproteins involved in electron transfer in bioenergetics

Tunable Biomimetic Chalcogels with Fe4S4 Cores and [SnnS2n+2]4–(n = 1, 2, 4) Building Blocks for Solar Fuel Catalysis

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Product

Resources

About

Tunable Biomimetic Chalcogels with Fe₄S₄ Cores and [Sn_nS_2n+2]^4–(n = 1, 2, 4) Building Blocks for Solar Fuel Catalysis