An overview of the factors playing a role in cytochrome P450 monooxygenase and ferredoxin interactions

Chiliza, Zinhle Edith; Martínez‐Oyanedel, José; Syed, Khajamohiddin

doi:10.1007/s12551-020-00749-7

Cited by 15 publications

(20 citation statements)

References 42 publications

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“…Consequently, catalyzed reactions require electron donors like NADH or NADPH. Flavin or iron-sulfur proteins transfer electrons from NADH or NADPH to the P450-bound heme (Chiliza et al 2020 ; Li et al 2020 ).…”

Section: Production Of Biotechnological Important Proteins: Multiple Cytochrome P450 Suitable For Whole-cell Transformationsmentioning

confidence: 99%

The “beauty in the beast”—the multiple uses of Priestia megaterium in biotechnology

Biedendieck

Knuuti

Jahn

2021

Appl Microbiol Biotechnol

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Over 30 years, the Gram-positive bacterium Priestia megaterium (previously known as Bacillus megaterium) was systematically developed for biotechnological applications ranging from the production of small molecules like vitamin B12, over polymers like polyhydroxybutyrate (PHB) up to the in vivo and in vitro synthesis of multiple proteins and finally whole-cell applications. Here we describe the use of the natural vitamin B12 (cobalamin) producer P. megaterium for the elucidation of the biosynthetic pathway and the subsequent systematic knowledge-based development for production purposes. The formation of PHB, a natural product of P. megaterium and potential petro-plastic substitute, is covered and discussed. Further important biotechnological characteristics of P. megaterium for recombinant protein production including high protein secretion capacity and simple cultivation on value-added carbon sources are outlined. This includes the advanced system with almost 30 commercially available expression vectors for the intracellular and extracellular production of recombinant proteins at the g/L scale. We also revealed a novel P. megaterium transcription-translation system as a complementary and versatile biotechnological tool kit. As an impressive biotechnology application, the formation of various cytochrome P450 is also critically highlighted. Finally, whole cellular applications in plant protection are completing the overall picture of P. megaterium as a versatile giant cell factory. Key points • The use of Priestia megaterium for the biosynthesis of small molecules and recombinant proteins through to whole-cell applications is reviewed. • P. megaterium can act as a promising alternative host in biotechnological production processes.

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Section: Production Of Biotechnological Important Proteins: Multiple Cytochrome P450 Suitable For Whole-cell Transformationsmentioning

confidence: 99%

The “beauty in the beast”—the multiple uses of Priestia megaterium in biotechnology

Biedendieck

Knuuti

Jahn

2021

Appl Microbiol Biotechnol

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“…Interdomain electrostatic interactions and redox potentials and distance between redox centers are proposed to influence the ET efficiency of this type of P450s. [49,57] Structural studies of P450cam/Pdx complex using crystallography and paramagnetic NMR spectroscopy suggest that Pdx binds to the P450 domain with the [2Fe-2S] cluster closely approaching the proximal side of heme (Figure 3A). [58] The similar domain arrangement is observed in human CYP11 A1/Adx complex [59] (Figure 3A).…”

Section: Class I Systemmentioning

confidence: 99%

“…P450s that use single‐electron carrier [2Fe‐2S] cluster to relay electrons is the most extensively studied class I systems. Interdomain electrostatic interactions and redox potentials and distance between redox centers are proposed to influence the ET efficiency of this type of P450s [49,57] . Structural studies of P450cam/Pdx complex using crystallography and paramagnetic NMR spectroscopy suggest that Pdx binds to the P450 domain with the [2Fe‐2S] cluster closely approaching the proximal side of heme (Figure 3A) [58] .…”

Section: The Electron Transfer Mechanism Of Multicomponent P450smentioning

confidence: 99%

Advanced Understanding of the Electron Transfer Pathway of Cytochrome P450s

et al. 2020

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Cytochrome P450s are heme‐thiolate enzymes that participate in carbon source assimilation, natural compound biosynthesis and xenobiotic metabolism in all kingdoms of life. P450s can catalyze various reactions by using a wide range of organic compounds, thus exhibiting great potential in biotechnological applications. The catalytic reactions of P450s are driven by electron equivalents that are sourced from pyridine nucleotides and delivered by cognate or matching redox partners (RPs). The electron transfer (ET) route from RPs to P450s involves one or more redox center‐containing domains. As the rate of ET is one of the main determinants of P450 efficacy, an in‐depth understanding of the P450 ET pathway should increase our knowledge of these important enzymes and benefit their further applications. Here, the various P450 RP systems along with current understanding of their ET routes will be reviewed. Notably, state‐of‐the‐art structural studies of the two main types of self‐sufficient P450 will also be summarized.

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“…The electron-transfer ability of ferredoxins to many proteins, including cytochrome P450 monooxygenases (CYPs/P450s) has been well established [7][8][9][10]. P450s are hemethiolate proteins ubiquitously present in organisms across biological kingdoms [11].…”

Section: Introductionmentioning

confidence: 99%

“…The well-known and well-studied ferredoxins include human ferredoxin known as adrenodoxin [22,23], ferredoxin from Pseudomonas putida known as putidaredoxin [24] and ferredoxin 1 (FDX1) from plants [25]. Ferredoxins belonging to different Fe-S cluster types have been crystallized, and some progress in understanding their interactions with P450s has been reported [7][8][9]26].…”

Section: Introductionmentioning

confidence: 99%

Diversification of Ferredoxins across Living Organisms

Nzuza

Padayachee

Chen

et al. 2021

CIMB

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Ferredoxins, iron-sulfur (Fe-S) cluster proteins, play a key role in oxidoreduction reactions. To date, evolutionary analysis of these proteins across the domains of life have been confined to observing the abundance of Fe-S cluster types (2Fe-2S, 3Fe-4S, 4Fe-4S, 7Fe-8S (3Fe-4s and 4Fe-4S) and 2[4Fe-4S]) and the diversity of ferredoxins within these cluster types was not studied. To address this research gap, here we propose a subtype classification and nomenclature for ferredoxins based on the characteristic spacing between the cysteine amino acids of the Fe-S binding motif as a subtype signature to assess the diversity of ferredoxins across the living organisms. To test this hypothesis, comparative analysis of ferredoxins between bacterial groups, Alphaproteobacteria and Firmicutes and ferredoxins collected from species of different domains of life that are reported in the literature has been carried out. Ferredoxins were found to be highly diverse within their types. Large numbers of alphaproteobacterial species ferredoxin subtypes were found in Firmicutes species and the same ferredoxin subtypes across the species of Bacteria, Archaea, and Eukarya, suggesting shared common ancestral origin of ferredoxins between Archaea and Bacteria and lateral gene transfer of ferredoxins from prokaryotes (Archaea/Bacteria) to eukaryotes. This study opened new vistas for further analysis of diversity of ferredoxins in living organisms.

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An overview of the factors playing a role in cytochrome P450 monooxygenase and ferredoxin interactions

Cited by 15 publications

References 42 publications

The “beauty in the beast”—the multiple uses of Priestia megaterium in biotechnology

The “beauty in the beast”—the multiple uses of Priestia megaterium in biotechnology

Advanced Understanding of the Electron Transfer Pathway of Cytochrome P450s

Diversification of Ferredoxins across Living Organisms

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