Photosensitive Nitrile Hydratase from Rhodococcus sp. N-771.

Honda, Jun; Nagamune, Teruyuki; Teratani, Yoshitaka; Hirata, Akira; Sasabe, Hiroyuki; Endo, Itaru

doi:10.1111/j.1749-6632.1992.tb32655.x

Cited by 6 publications

(10 citation statements)

References 7 publications

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“…It is presumed that these amino acid residues are involved in interactions with the iron atoms and/or their ligands. Interestingly, Ser and Thr are present in the putative iron binding site of the a subunit [8] with the sequence -Cys, ,,-Ser-Leu-Cys-Ser-CysThr,,,- [2,6,7]. Also, relatively small band intensities in the amide I region (1700-1600 cm-') ( Fig.…”

Section: Resultsmentioning

confidence: 99%

“…NHase from Rhodococcu.v sp. N-771, which consists of two subunits, a (M, = 22,787) and B (M, = 23,428) [2], possesses two non-heme iron atoms as cofactors [3], and shows a unique manner of photoactivation, i.e. the enzyme is activated by light irradiation [4,5].…”

Section: Introductionmentioning

confidence: 99%

“…N-774 and Brevihacterium sp. R312, because the amino acid sequences are identical among the three [2,6,7]. Although various spectroscopies, including EXAFS [8], EPR [9], ENDOR [IO], resonance Raman [8], and Miissbauer [3], have been applied to the NHase from these bacteria, the detailed structure of the di-iron center has not been clarified yet.…”

Section: Introductionmentioning

confidence: 99%

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Photosensitive nitrile hydratase intrinsically possesses nitric oxide bound to the non‐heme iron center: evidence by Fourier transform infrared spectroscopy

et al. 1995

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Nitrile hydratase (NHase) from Rhodococcus sp. N-771 is a photosensitive enzyme that catalyzes hydration of nitriles to the corresponding amides. Light-induced Fourier transform infrared difference spectra between the inactive and active forms of NHase were measured with both the natural (14N) and "Nlabeled NHases. The results showed, for the first time, that NHase intrinsically possesses nitric oxide (NO) molecules bound to the non-heme iron center. The possible role of NO in the photoactivation process of NHase is discussed.

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Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Photosensitive nitrile hydratase intrinsically possesses nitric oxide bound to the non‐heme iron center: evidence by Fourier transform infrared spectroscopy

et al. 1995

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“…al., 1991) and R. sp. N-771 (Honda et al, 1992a). In addition, we have observed that the NHase activity of B. R3 12 invivo is affected by light irradiation (unpublished results).…”

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confidence: 79%

Spectroscopic Observation of the Intramolecular Electron Transfer in the Photoactivation Processes of Nitrile Hydratase

Honda

Kandori²,

Okada³

et al. 1994

Biochemistry

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The photoactivation phenomena of the photosensitive enzyme nitrile hydratase (NHase) was studied by various spectroscopic methods. We have already shown that the photoactivation of NHase accompanies oxidation of an iron atom in the NHase [Honda et al. (1992) FEBS Lett. 301, 177-180]. From the results obtained in the present study by absorption, action, and fluorescence spectra, we show that the chromophore responsible for the photoactivation process is the iron complex, and the tryptophan residues in NHase induce the oxidation of the iron atom via an energy-transfer process. The nanosecond flash photolysis experiment revealed that this photoactivation process is completed within 50 ns, which suggests that the changes observable in the absorption spectra originate from an intramolecular electron transfer occurring from an electronically excited state. Also the role of a stabilizing reagent, namely, n-butyric acid (BA), was investigated using the above methods, which revealed that BA, besides its stabilizing effect, contributes to the increase in apparent photoactivation rate.

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“…F28; JCM3095: Pseudonocardia thermophila JCM3095[33]; R1: Rhodococcus erythropolis[34]; P1: Pseudomonas chlororaphis[35]; N-771: Rhodococcus sp. N-771[36].…”

mentioning

confidence: 98%

Nitrile hydratase from Mesorhizobium sp. F28 and its potential for nitrile biotransformation

Feng

Chen

Wen

et al. 2008

Process Biochemistry

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Photosensitive Nitrile Hydratase from Rhodococcus sp. N-771.

Cited by 6 publications

References 7 publications

Photosensitive nitrile hydratase intrinsically possesses nitric oxide bound to the non‐heme iron center: evidence by Fourier transform infrared spectroscopy

Photosensitive nitrile hydratase intrinsically possesses nitric oxide bound to the non‐heme iron center: evidence by Fourier transform infrared spectroscopy

Spectroscopic Observation of the Intramolecular Electron Transfer in the Photoactivation Processes of Nitrile Hydratase

Nitrile hydratase from Mesorhizobium sp. F28 and its potential for nitrile biotransformation

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