The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
The catalytic pathway of horseradish peroxidase at high resolution
Open accessAbstract
A molecular description of oxygen and peroxide activation in biological systems is difficult, because electrons liberated during X-ray data collection reduce the active centres of redox enzymes catalysing these reactions. Here we describe an effective strategy to obtain crystal structures for high-valency redox intermediates and present a three-dimensional movie of the X-ray-driven catalytic reduction of a bound dioxygen species in horseradish peroxidase (HRP). We also describe separate experiments in which high-resolution structures could be obtained for all five oxidation states of HRP, showing such structures with preserved redox states for the first time.
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Cites
Potential for biomolecular imaging with femtosecond X-ray pulses
Neutze, R., Wouts, R., van der Spoel, D., Weckert, E., & Hajdu, J. (2000) · Nature · doi:10.1038/35021099 · Cited by 2,022
Self-citationComet Hyakutake x‐ray source: Charge transfer of solar wind heavy ions
Cravens, T. E. (1997) · Geophysical Research Letters · doi:10.1029/96gl03780 · Cited by 469
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Poulos, T. L. (2014) · Chemical Reviews · doi:10.1021/cr400415k · Cited by 1,443
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Martell, J. D., Deerinck, T. J., Sancak, Y., Poulos, T. L., Mootha, V. K., Sosinsky, G. E., Ellisman, M. H., & Ting, A. Y. (2012) · Nature Biotechnology · doi:10.1038/nbt.2375 · Cited by 722
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Horseradish peroxidase: a valuable tool in biotechnology
Azevedo, A. M., Martins, V. C., Prazeres, D. M. F., Vojinović, V., Cabral, J. M. S., & Fonseca, L. P. (2003) · Biotechnology Annual Review · doi:10.1016/s1387-2656(03)09003-3 · Cited by 243
Redox properties of heme peroxidases
Battistuzzi, G., Bellei, M., Bortolotti, C. A., & Sola, M. (2010) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2010.03.002 · Cited by 218
Cobamide-mediated enzymatic reductive dehalogenation via long-range electron transfer
Kunze, C., Bommer, M., Hagen, W. R., Uksa, M., Dobbek, H., Schubert, T., & Diekert, G. (2017) · Nature Communications · doi:10.1038/ncomms15858 · Cited by 104
Crystal Structure of the Dioxygen-bound Heme Oxygenase from Corynebacterium diphtheriae
Unno, M., Matsui, T., Chu, G. C., Couture, M., Yoshida, T., Rousseau, D. L., Olson, J. S., & Ikeda-Saito, M. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m400491200 · Cited by 83
Chemiexcited neurotransmitters and hormones create DNA photoproducts in the dark
Gonçalves, L. C. P., Angelé-Martínez, C., Premi, S., Palmatier, M. A., Prado, F. M., Di Mascio, P., Bastos, E. L., & Brash, D. E. (2023) · ACS Chemical Biology · doi:10.1021/acschembio.2c00787 · Cited by 15
Metadata
- Authors
- Berglund, G. I., Carlsson, G. H., Smith, A. T., Szöke, H., Henriksen, A., & Hajdu, J.
- Venue
- Nature
- Published
- 2002-05
- Volume
- 417
- Issue
- 6887
- Pages
- 463-468
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W2138393107
- Cited by
- 956
- References
- 2
- FWCI
- 20.82
- Type
- journal article
- Language
- en
- Open access
- green
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