Functional plasticity and catalytic efficiency in plant and bacterial ferredoxin-NADP(H) reductases

Ceccarelli, Eduardo A.; Arakaki, Adrián K.; Cortez, Néstor; Carrillo, Néstor

doi:10.1016/j.bbapap.2003.12.005

Cited by 137 publications

(183 citation statements)

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“…The turnover number of B. subtilis FNR for NADP(H) was 35.4 s -1 (Table 2) which is slightly smaller than those of plastidic FNRs, but considerably larger than those from A. vinelandii and E. coli (Ceccarelli et al 2004). …”

Section: Discussionmentioning

confidence: 90%

“…Fd-NAD(P) + reductase (FNR) (EC 1.18.1.2 and EC 1.18.1.3 with NADP + and NAD + as the substrate, respectively) (Ceccarelli et al 2004). The catalytic electron transport function between NAD(P)H and an artificial electron acceptor such as methyl viologen and 2,6-dichlorophenol-indophenol (DPIP) is called diaphorase activity and is shown by FNRs.…”

Section: The Enzymes That Mediate the Redox Reactions Between Nad(p) mentioning

confidence: 99%

“…The second group is sometimes called the bacteria type and is composed of monomeric FNRs from some bacteria such as Escherichia coli (Bianchi et al 1993) and Azotobacter vinelandii (Isas et al 1995). There are significant similarities between these two groups of FNRs in 3-D structure (Prasad et al 1998) as well as in amino acid sequence (Arakaki et al 1997, Ceccarelli et al 2004). These two FNR groups can be united to a plant type in a broader sense.…”

Section: The Enzymes That Mediate the Redox Reactions Between Nad(p) mentioning

confidence: 99%

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Purification and characterization of ferredoxin-NADP+ reductase encoded by Bacillus subtilis yumC

2004

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From Bacillus subtilis cell extracts, ferredoxin-NADP + reductase (FNR) was purified to homogeneity and found to be the yumC gene product by N-terminal amino acid sequencing. YumC is a ~94 kDa homodimeric protein with one molecule of non-covalently bound FAD per subunit. In a diaphorase assay with 2,6-dichlorophenol-indophenol as an electron acceptor, the affinity to NADPH was much higher than to NADH, with K m values of 0.57 vs. >200 µM. K cat values of YumC with NADPH were 22.7 and 35.4 s -1 in diaphorase and in a ferredoxin-dependent NADPH-cytochrome c reduction assay, respectively. The cell extracts contained another diaphorase-active enzyme, the yfkO gene product, but its affinity for ferredoxin was very low. The deduced YumC amino acid sequence has high identity to that of the recently identified Chlorobium tepidum FNR. A genomic database search indicated that there are more than 20 genes encoding proteins that share a high level of amino acid sequence identity with YumC and annotated variously as NADH oxidase, thioredoxin reductase, thioredoxin reductase-like protein, etc. These genes are found notably in Gram-positive bacteria except for Clostridia, and less frequently in archaea and proteobacteria. We propose that YumC and C. tepidum FNR constitute a new group of FNR which should be added to the already established plant type, bacteria type, and mitochondria type FNR groups.

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Section: Discussionmentioning

confidence: 90%

Section: The Enzymes That Mediate the Redox Reactions Between Nad(p) mentioning

confidence: 99%

Section: The Enzymes That Mediate the Redox Reactions Between Nad(p) mentioning

confidence: 99%

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Purification and characterization of ferredoxin-NADP+ reductase encoded by Bacillus subtilis yumC

2004

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“…reaction (Bruns and Karplus, 1995;Carrillo and Ceccarelli, 2003). Whereas many functional properties of FNR have been thoroughly characterized (Carrillo and Ceccarelli, 2003;Ceccarelli et al, 2004), until recently, little was known on the actual contribution of this flavoenzyme to electron transport and photosynthesis in planta. The combined use of FNR antisense (Hajirezaei et al, 2002) and overexpressing transgenic plants (this work) revealed somehow paradoxical behavior.…”

Section: Discussionmentioning

confidence: 99%

“…This function depends on the NADPH-Fd reductase activity of FNR, which proceeds backward with respect to the physiological photosynthetic direction and is expected to occur only rarely in illuminated leaves. However, this is the most extended function of FNRs in nature, taking place in plant roots and other heterotrophic tissues and organisms (for review, see Ceccarelli et al, 2004). When FNR is expressed in transgenic plants, a considerable fraction of the enzyme accumulates in the stroma (Fig.…”

Section: Photosynthesis In Fnr-mentioning

confidence: 99%

Transgenic Tobacco Plants Overexpressing Chloroplastic Ferredoxin-NADP(H) Reductase Display Normal Rates of Photosynthesis and Increased Tolerance to Oxidative Stress

et al. 2006

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(M.P., H.T., M.-R.H.)Ferredoxin-NADP(H) reductase (FNR) catalyzes the last step of photosynthetic electron transport in chloroplasts, driving electrons from reduced ferredoxin to NADP 1 . This reaction is rate limiting for photosynthesis under a wide range of illumination conditions, as revealed by analysis of plants transformed with an antisense version of the FNR gene. To investigate whether accumulation of this flavoprotein over wild-type levels could improve photosynthetic efficiency and growth, we generated transgenic tobacco (Nicotiana tabacum) plants expressing a pea (Pisum sativum) FNR targeted to chloroplasts. The alien product distributed between the thylakoid membranes and the chloroplast stroma. Transformants grown at 150 or 700 mmol quanta m 22 s 21 displayed wild-type phenotypes regardless of FNR content. Thylakoids isolated from plants with a 5-fold FNR increase over the wild type displayed only moderate stimulation (approximately 20%) in the rates of electron transport from water to NADP 1 . In contrast, when donors of photosystem I were used to drive NADP 1 photoreduction, the activity was 3-to 4-fold higher than the wild-type controls. Plants expressing various levels of FNR (from 1-to 3.6-fold over the wild type) failed to show significant differences in CO 2 assimilation rates when assayed over a range of light intensities and CO 2 concentrations. Transgenic lines exhibited enhanced tolerance to photooxidative damage and redox-cycling herbicides that propagate reactive oxygen species. The results suggest that photosynthetic electron transport has several rate-limiting steps, with FNR catalyzing just one of them.

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The extremophilic Andean isolate Acinetobacter sp. Ver3 expresses two ferredoxin‐NADP⁺ reductase isoforms with different catalytic properties

Palavecino,

Sartorio,

Carrillo

et al. 2024

FEBS Letters

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Ferredoxin/flavodoxin‐NADPH reductases (FPRs) catalyze the reversible electron transfer between NADPH and ferredoxin/flavodoxin. The Acinetobacter sp. Ver3 isolated from high‐altitude Andean lakes contains two isoenzymes, FPR1ver3 and FPR2ver3. Absorption spectra of these FPRs revealed typical features of flavoproteins, consistent with the use of FAD as a prosthetic group. Spectral differences indicate distinct electronic arrangements for the flavin in each enzyme. Steady‐state kinetic measurements show that the enzymes display catalytic efficiencies in the order of 1–6 μm−1·s−1, although FPR1ver3 exhibited higher kcat values compared to FPR2ver3. When flavodoxinver3 was used as a substrate, both reductases exhibited dissimilar behavior. Moreover, only FPR1ver3 is induced by oxidative stimuli, indicating that the polyextremophile Ver3 has evolved diverse strategies to cope with oxidative environments.

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Functional plasticity and catalytic efficiency in plant and bacterial ferredoxin-NADP(H) reductases

Cited by 137 publications

References 74 publications

Purification and characterization of ferredoxin-NADP+ reductase encoded by Bacillus subtilis yumC

Purification and characterization of ferredoxin-NADP+ reductase encoded by Bacillus subtilis yumC

Transgenic Tobacco Plants Overexpressing Chloroplastic Ferredoxin-NADP(H) Reductase Display Normal Rates of Photosynthesis and Increased Tolerance to Oxidative Stress

The extremophilic Andean isolate Acinetobacter sp. Ver3 expresses two ferredoxin‐NADP⁺ reductase isoforms with different catalytic properties

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Functional plasticity and catalytic efficiency in plant and bacterial ferredoxin-NADP(H) reductases

Cited by 137 publications

References 74 publications

Purification and characterization of ferredoxin-NADP+ reductase encoded by Bacillus subtilis yumC

Purification and characterization of ferredoxin-NADP+ reductase encoded by Bacillus subtilis yumC

Transgenic Tobacco Plants Overexpressing Chloroplastic Ferredoxin-NADP(H) Reductase Display Normal Rates of Photosynthesis and Increased Tolerance to Oxidative Stress

The extremophilic Andean isolate Acinetobacter sp. Ver3 expresses two ferredoxin‐NADP+ reductase isoforms with different catalytic properties

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The extremophilic Andean isolate Acinetobacter sp. Ver3 expresses two ferredoxin‐NADP⁺ reductase isoforms with different catalytic properties