The apicomplexan <i>Cryptosporidium parvum</i> possesses a single mitochondrial‐type ferredoxin and ferredoxin:NADP<sup>+</sup> reductase system

Cheng, Lei; Rider, S. Dean; Cai, Wei; Zhang, Haili; Tan, Xiangshi; Zhu, Guangxi

doi:10.1002/pro.487

Cited by 6 publications

(4 citation statements)

References 39 publications

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“…Across each Fe–S cluster type, Fds can be partitioned into additional categories (Table ) based on structural, functional, and phylogenetic relationships. The 2Fe2S Fds have been classically differentiated into nine categories, including the plant-leaf, plant-root, hydrogenosomal, eukaryotic-P450, eukaryotic-ISC, prokaryotic-P450, prokaryotic-ISC, nitrogenase-protecting, and thioredoxin-like types. − The 4Fe4S Fds have been sorted into seven categories, including the clostridial, alvin-like, hybrid 3Fe4S/4Fe4S, hybrid-Zn binding, photosystem, nitrogenase, and monocluster types. ,,− …”

Section: Sequence and Structure Relationships Of Ferredoxinsmentioning

confidence: 99%

Cellular Assays for Ferredoxins: A Strategy for Understanding Electron Flow through Protein Carriers That Link Metabolic Pathways

et al. 2016

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The ferredoxin (Fd) protein family is a structurally diverse group of iron-sulfur proteins that function as electron carriers, linking biochemical pathways important for energy transduction, nutrient assimilation, and primary metabolism. While considerable biochemical information about individual Fd protein electron carriers and their reactions has been acquired, we cannot yet anticipate the proportion of electrons shuttled between different Fd-partner proteins within cells using biochemical parameters that govern electron flow, such as holo-Fd concentration, midpoint potential (driving force), molecular interactions (affinity and kinetics), conformational changes (allostery), and off-pathway electron leakage (chemical oxidation). Herein, we describe functional and structural gaps in our Fd knowledge within the context of a sequence similarity network and phylogenetic tree, and we propose a strategy for improving our understanding of Fd sequence-function relationships. We suggest comparing the functions of divergent Fds within cells whose growth, or other measurable output, requires electron transfer between defined electron donor and acceptor proteins. By comparing Fd-mediated electron transfer with biochemical parameters that govern electron flow, we posit that models that anticipate energy flow across Fd interactomes can be built. This approach is expected to transform our ability to anticipate Fd control over electron flow in cellular settings, an obstacle to the construction of synthetic electron transfer pathways and rational optimization of existing energy-conserving pathways.

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Section: Sequence and Structure Relationships Of Ferredoxinsmentioning

confidence: 99%

Cellular Assays for Ferredoxins: A Strategy for Understanding Electron Flow through Protein Carriers That Link Metabolic Pathways

et al. 2016

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“…Then, the enzyme expression was induced with IPTG at a final concentration of 0.1 mM. When expressing FNR, 0.01 mM riboflavin was added 46 together with IPTG. The protein was expressed at 22 °C and 220 rpm for 10 h.…”

Section: ■ Materials and Methodsmentioning

confidence: 99%

A Minimized Synthetic Carbon Fixation Cycle

et al. 2021

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Natural CO 2 fixation cycles usually comprise multiple reactions, which may reduce the efficiency of the cycle. Here, we report the design and experimental demonstration of a minimized synthetic CO 2 fixation cycle which contains only four reactions. The cycle comprises pyruvate carboxylase, oxaloacetate acetylhydrolase, acetate-CoA ligase, and pyruvate synthase and is named the POAP cycle. The POAP cycle can condense two molecules of CO 2 into one molecule of oxalate in each step at the expense of two molecules of ATP and one reducing equivalent in the form of NAD(P)H. By identifying a ferredoxin from Hydrogenobacter thermophilus that can efficiently drive the rate-limiting reductive carboxylation step, the POAP cycle can be operated at 50 °C under anaerobic conditions, reaching a CO 2 fixation rate of 8.0 nmol CO 2 min −1 mg −1 CO 2 -fixing enzymes. The design and demonstration of the POAP cycle may provide a model to study CO 2 fixation in the earliest organisms.

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“…Apicomplexa and the early branching dinoflagellate Perkinsus all contain sequences encoding mitochondrial ferredoxin NADP reductase (FNR) (adrenodoxin NADP + oxidoreductase) ( Lei et al 2010 ). However, initial searches using the dinoflagellate EST libraries were only able to identify a putative FNR homolog which showed more similarity to the chloroplast isoform (cpFNR).…”

Section: Gene Duplications Are Commonmentioning

confidence: 99%

Identification of Sequences EncodingSymbiodinium minutumMitochondrial Proteins

2016

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The dinoflagellates are an extremely diverse group of algae closely related to the Apicomplexa and the ciliates. Much work has previously been undertaken to determine the presence of various biochemical pathways within dinoflagellate mitochondria. However, these studies were unable to identify several key transcripts including those encoding proteins involved in the pyruvate dehydrogenase complex, iron–sulfur cluster biosynthesis, and protein import. Here, we analyze the draft nuclear genome of the dinoflagellate Symbiodinium minutum, as well as RNAseq data to identify nuclear genes encoding mitochondrial proteins. The results confirm the presence of a complete tricarboxylic acid cycle in the dinoflagellates. Results also demonstrate the difficulties in using the genome sequence for the identification of genes due to the large number of introns, but show that it is highly useful for the determination of gene duplication events.

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The apicomplexan Cryptosporidium parvum possesses a single mitochondrial‐type ferredoxin and ferredoxin:NADP⁺ reductase system

Cited by 6 publications

References 39 publications

Cellular Assays for Ferredoxins: A Strategy for Understanding Electron Flow through Protein Carriers That Link Metabolic Pathways

Cellular Assays for Ferredoxins: A Strategy for Understanding Electron Flow through Protein Carriers That Link Metabolic Pathways

A Minimized Synthetic Carbon Fixation Cycle

Identification of Sequences EncodingSymbiodinium minutumMitochondrial Proteins

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The apicomplexan Cryptosporidium parvum possesses a single mitochondrial‐type ferredoxin and ferredoxin:NADP+ reductase system

Cited by 6 publications

References 39 publications

Cellular Assays for Ferredoxins: A Strategy for Understanding Electron Flow through Protein Carriers That Link Metabolic Pathways

Cellular Assays for Ferredoxins: A Strategy for Understanding Electron Flow through Protein Carriers That Link Metabolic Pathways

A Minimized Synthetic Carbon Fixation Cycle

Identification of Sequences EncodingSymbiodinium minutumMitochondrial Proteins

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The apicomplexan Cryptosporidium parvum possesses a single mitochondrial‐type ferredoxin and ferredoxin:NADP⁺ reductase system