Introduction, J.C. Spain Strategies for Aerobic Degradation of Nitroaromatic Compounds by Bacteria: Process Discovery to Field Application, S.F. Nishimo, J.C. Spain, and Z. He Molecular Biology of Nitroarene Degradation, R.E. Parales Perspectives of Bioelimination of Polynitroaromatic Compounds, H. Lenke, C. Achtnich, and H-J. Knackmuss Identification of Genes Involved in Picric Acid and 2,4-Dinitrophenol Degradation by mRNA Differential Display, R. Ross, D.M. Walters, H-J. Knackmuss, and P.E. Rouviere Microbial Degradation of Mononitrophenols and Mononitrobenzoates, G.J. Zylstra, S-W. Bang, L.M. Newman, and L.L. Perry The Role of Nitrate Ester Reductase Enzymes in the Biodegradation of Explosives, R.E. Williams and N.C. Bruce Anaerobic Transformation of TNT by Clostridium, F. Ahmad and J.B. Hughes Fungal Degradation of Explosives: TNT and Related Nitroaromatic Compounds, W. Fritsche, K. Scheibner, A. Herre, and M. Hofrichter Phytoremediation and Plant Metabolism of Explosives and Nitroaromatic Compounds, J.G. Burken, J.V. Shanks, and P.L. Thompson Biodegradation of RDX and HMX: From Basic Research to Field Application, J. Hawari Subsurface Chemistry of Nitroaromatic Compounds, S.B. Haderlein, T.B. Hofstetter, and R.P. Schwartzenbach Composting (Humification) of Nitroaromatic Compounds, D. Bruns-Nagel, K. Steinbach, D.Gemsa, and E. von Low Application and Costs for Biological Treatment of Explosive-Contaminated Soils in the United States, D.E. Jerger and P.M. Woodhull

Biodegradation of Nitroaromatic Compounds and Explosives

All oxygenic photosynthetically derived reducing equivalents are utilized by combinations of a single multifuctional electron carrier protein, ferredoxin (Fd), and several Fd-dependent oxidoreductases. We report the first crystal structure of the complex between maize leaf Fd and Fd-NADP(+) oxidoreductase (FNR). The redox centers in the complex--the 2Fe-2S cluster of Fd and flavin adenine dinucleotide (FAD) of FNR--are in close proximity; the shortest distance is 6.0 A. The intermolecular interactions in the complex are mainly electrostatic, occurring through salt bridges, and the interface near the prosthetic groups is hydrophobic. NMR experiments on the complex in solution confirmed the FNR recognition sites on Fd that are identified in the crystal structure. Interestingly, the structures of Fd and FNR in the complex and in the free state differ in several ways. For example, in the active site of FNR, Fd binding induces the formation of a new hydrogen bond between side chains of Glu 312 and Ser 96 of FNR. We propose that this type of molecular communication not only determines the optimal orientation of the two proteins for electron transfer, but also contributes to the modulation of the enzymatic properties of FNR.

Structure of the electron transfer complex between ferredoxin and ferredoxin-NADP + reductase

The old yellow enzyme (OYE) family is a large group of flavin-dependent redox biocatalysts with major applications in the industrial reduction of activated alkenes. These enzymes have broad specificity, are relatively stable, and have been made available in large quantities by using conventional genetic methods. The catalytic cycle comprises two half-reactions: reduction of flavin mononucleotide by NAD(P)H followed by flavin oxidation through stereospecific reduction of the CC bond of a wide range of activated alkenes. Recent years have witnessed extensive investigation of these reactions, aided by knowledge of atomic resolution structures for selected family members. In turn, this has led to deep understanding of the stereochemical course of substrate reduction and expansion of the biocatalytic versatility of this enzyme family through engineering approaches. We provide an overview of the structures, mechanisms, and chemical specificity of the reactions catalyzed by the OYE members. We provide an overview of the biocatalytic potential of this family of enzymes and illustrate the value of combining mechanistic and structural studies of biocatalysts to guide future exploitation of these enzymes in industrial biocatalysis.

Biocatalytic Reductions and Chemical Versatility of the Old Yellow Enzyme Family of Flavoprotein Oxidoreductases

Ferredoxin (Fd) is a small [2Fe-2S] cluster-containing protein found in all organisms performing oxygenic photosynthesis. Fd is the first soluble acceptor of electrons on the stromal side of the chloroplast electron transport chain, and as such is pivotal to determining the distribution of these electrons to different metabolic reactions. In chloroplasts, the principle sink for electrons is in the production of NADPH, which is mostly consumed during the assimilation of CO2 . In addition to this primary function in photosynthesis, Fds are also involved in a number of other essential metabolic reactions, including biosynthesis of chlorophyll, phytochrome and fatty acids, several steps in the assimilation of sulphur and nitrogen, as well as redox signalling and maintenance of redox balance via the thioredoxin system and Halliwell-Asada cycle. This makes Fds crucial determinants of the electron transfer between the thylakoid membrane and a variety of soluble enzymes dependent on these electrons. In this article, we will first describe the current knowledge on the structure and function of the various Fd isoforms present in chloroplasts of higher plants and then discuss the processes involved in oxidation of Fd, introducing the corresponding enzymes and discussing what is known about their relative interaction with Fd.

https://onlinelibrary.wiley.com/doi/pdf/10.1111/pce.12046

Plant type ferredoxins and ferredoxin‐dependent metabolism

NO synthase: structures and mechanisms.

The flavoenzyme ferredoxin-NADP+ reductase (FNR) catalyzes the production of NADPH during photosynthesis. Whereas the structures of FNRs from spinach leaf and a cyanobacterium as well as many of their homologs have been solved, none of these studies has yielded a productive geometry of the flavin-nicotinamide interaction. Here, we show that this failure occurs because nicotinamide binding to wild type FNR involves the energetically unfavorable displacement of the C-terminal Tyr side chain. We used mutants of this residue (Tyr 308) of pea FNR to obtain the structures of productive NADP+ and NADPH complexes. These structures reveal a unique NADP+ binding mode in which the nicotinamide ring is not parallel to the flavin isoalloxazine ring, but lies against it at an angle of approximately 30 degrees, with the C4 atom 3 A from the flavin N5 atom.

A productive NADP+ binding mode of ferredoxin-NADP+ reductase revealed by protein engineering and crystallographic studies.

On the active site of Old Yellow Enzyme. Role of histidine 191 and asparagine 194.

Probing the function of the invariant glutamyl residue 312 in spinach ferredoxin-NADP+ reductase.

reductase revealed by protein engineering and crystallographic studies

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A productive NADP+ binding mode of ferredoxin-NADP+ reductase revealed by protein engineering and crystallographic studies.

On the active site of Old Yellow Enzyme. Role of histidine 191 and asparagine 194.

Probing the function of the invariant glutamyl residue 312 in spinach ferredoxin-NADP+ reductase.

reductase revealed by protein engineering and crystallographic studies