NDLI: NO binding to naphthalene dioxygenase

Content Provider	Springer Nature Link
Author	Karlsson, Andreas Parales, Juan V. Parales, Rebecca E. Gibson, David T. Eklund, Hans Ramaswamy, S.
Copyright Year	2005
Abstract	Nitric oxide (NO) is commonly used as an analogue for dioxygen in structural and spectroscopic studies of oxygen binding and oxygen activation. In this study, crystallographic structures of naphthalene dioxygenase (NDO) in complex with nitric oxide are reported. In the presence of the aromatic substrate indole, NO is bound end-on to the active-site mononuclear iron of NDO. The structural observations correlate well with spectroscopic measurements of NO binding to NDO in solution. However, the end-on binding of NO is in contrast to the recently reported structure of oxygen to the active-site iron of NDO that binds side-on. While NO is a good oxygen analogue with many similarities to O2, the different binding mode of NO to the active-site iron atom leads to different mechanistic implications. Hence, caution needs to be used in extrapolating NO as an analogue to O2 binding.
Starting Page	483
Ending Page	489
Page Count	7
File Format	PDF
ISSN	09498257
Journal	JBIC Journal of Biological Inorganic Chemistry
Volume Number	10
Issue Number	5
e-ISSN	14321327
Language	English
Publisher	Springer-Verlag
Publisher Date	2005-06-08
Publisher Place	Berlin, Heidelberg
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Rieske dioxygenase Nitric oxide Iron Crystal structures Indole
Content Type	Text
Resource Type	Article
Subject	Biochemistry Inorganic Chemistry

Sl.	Authority	Responsibilities	Communication Details
1	Ministry of Education (GoI), Department of Higher Education	Sanctioning Authority	https://www.education.gov.in/ict-initiatives
2	Indian Institute of Technology Kharagpur	Host Institute of the Project: The host institute of the project is responsible for providing infrastructure support and hosting the project	https://www.iitkgp.ac.in
3	National Digital Library of India Office, Indian Institute of Technology Kharagpur	The administrative and infrastructural headquarters of the project	Dr. B. Sutradhar bsutra@ndl.gov.in
4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
5	Website/Portal (Helpdesk)	Queries regarding NDLI and its services	support@ndl.gov.in
6	Contents and Copyright Issues	Queries related to content curation and copyright issues	content@ndl.gov.in
7	National Digital Library of India Club (NDLI Club)	Queries related to NDLI Club formation, support, user awareness program, seminar/symposium, collaboration, social media, promotion, and outreach	clubsupport@ndl.gov.in
8	Digital Preservation Centre (DPC)	Assistance with digitizing and archiving copyright-free printed books	dpc@ndl.gov.in
9	IDR Setup or Support	Queries related to establishment and support of Institutional Digital Repository (IDR) and IDR workshops	idr@ndl.gov.in

NO binding to Mn-substituted homoprotocatechuate 2,3-dioxygenase: relationship to O2 reactivity

Nitrite binding to metmyoglobin and methemoglobin in comparison to nitric oxide binding

Iron nitrosyl complexes as models for biological nitric oxide transfer reagents

Modulation of NO binding to cytochrome c′ by distal and proximal haem pocket residues

The “Bridging” Aspartate 178 in Phthalate Dioxygenase Facilitates Interactions between the Rieske Center and the Iron(II)−Mononuclear Center

A study of NO trafficking from dinitrosyl–iron complexes to the recombinant E. coli transcriptional factor SoxR

Binding of nitrite and its reductive activation to nitric oxide at biomimetic copper centers

Exploring substrate binding in homoprotocatechuate 2,3-dioxygenase using isothermal titration calorimetry

Crystal structures of Streptococcus pyogenes Dpr reveal a dodecameric iron-binding protein with a ferroxidase site

NO binding to naphthalene dioxygenase

Similar Documents

NO binding to Mn-substituted homoprotocatechuate 2,3-dioxygenase: relationship to O2 reactivity

Nitrite binding to metmyoglobin and methemoglobin in comparison to nitric oxide binding

Iron nitrosyl complexes as models for biological nitric oxide transfer reagents

Modulation of NO binding to cytochrome c′ by distal and proximal haem pocket residues

The “Bridging” Aspartate 178 in Phthalate Dioxygenase Facilitates Interactions between the Rieske Center and the Iron(II)−Mononuclear Center

A study of NO trafficking from dinitrosyl–iron complexes to the recombinant E. coli transcriptional factor SoxR

Binding of nitrite and its reductive activation to nitric oxide at biomimetic copper centers

Exploring substrate binding in homoprotocatechuate 2,3-dioxygenase using isothermal titration calorimetry

Crystal structures of Streptococcus pyogenes Dpr reveal a dodecameric iron-binding protein with a ferroxidase site

NO binding to naphthalene dioxygenase