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We began analyzing https://link.springer.com/chapter/10.1007/978-1-4615-2960-6_73, but it redirected us to https://link.springer.com/chapter/10.1007/978-1-4615-2960-6_73. The analysis below is for the second page.

Title[redir]:
Reduced Pterins as Scavengers for Reactive Oxygen Species | SpringerLink
Description:
Pterins are widely distributed in nature in three forms: tetrahydro, dihydro, and oxidized. The most studied pterin is L-erythro-5,6,7,8-tetrahydrobiopterin (BH4), the electron donor for mixed function oxidases, such as Phe hydroxylase during the conversion of Phe to...

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Keywords {🔍}

chapter, google, scholar, article, cas, biology, medicine, usa, privacy, cookies, content, information, publish, shen, zhang, download, springer, search, chemistry, pterins, preview, college, function, personal, data, log, journal, research, pteridines, folates, oxygen, yixian, book, nature, nitric, oxide, dihydropteridine, reductase, dhpr, access, pubmed, author, texas, south, alabama, mobile, ebook, usd, optional, analysis,

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month download article/chapter cas google scholar reactive oxygen species privacy choices/manage cookies device instant download google scholar download preview pdf european economic area biogenic amine synthesis synthesize catecholamine neurotransmitters journal finder publish human biological chemistry conditions privacy policy nitric oxide synthase produces nitric oxide accepting optional cookies mixed function oxidases texas medical branch main content log chapter cite chapter shen book series chapter usd 29 social media permissions reprints chapter chemistry information zhang journal publish dihydropteridine reductase reduced pterins privacy policy check access oxygen activation ethics access baugh rights ma chapter log books a nitric oxide optional cookies personal data manage preferences usa authors usa june usa charles 7-dihydropteridine oxidoreductase data protection essential cookies cookies skip

Schema {🗺️}

ScholarlyArticle:
      headline:Reduced Pterins as Scavengers for Reactive Oxygen Species
      pageEnd:354
      pageStart:351
      image:https://media.springernature.com/w153/springer-static/cover/book/978-1-4615-2960-6.jpg
      genre:
         Biomedical and Life Sciences
         Biomedical and Life Sciences (R0)
      isPartOf:
         name:Chemistry and Biology of Pteridines and Folates
         isbn:
            978-1-4615-2960-6
            978-1-4613-6287-6
         type:Book
      publisher:
         name:Springer US
         logo:
            url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
            type:ImageObject
         type:Organization
      author:
            name:Rong-sen Shen
            affiliation:
                  name:The University of Texas Medical Branch
                  address:
                     name:Department of Human Biological Chemistry and Genetics, The University of Texas Medical Branch, Galveston, USA
                     type:PostalAddress
                  type:Organization
            type:Person
            name:Yixian Zhang
            affiliation:
                  name:The University of Texas Medical Branch
                  address:
                     name:Department of Human Biological Chemistry and Genetics, The University of Texas Medical Branch, Galveston, USA
                     type:PostalAddress
                  type:Organization
            type:Person
      keywords:Nitric Oxide, Antioxidant System, Mixed Function Oxidase, Boric Acid Solution, Dihydropteridine Reductase
      description:Pterins are widely distributed in nature in three forms: tetrahydro, dihydro, and oxidized. The most studied pterin is L-erythro-5,6,7,8-tetrahydrobiopterin (BH4), the electron donor for mixed function oxidases, such as Phe hydroxylase during the conversion of Phe to Tyr, and Tyr and Trp hydroxylases during biogenic amine synthesis.1 BH4 also serves as the cofactor for nitric oxide synthase which produces nitric oxide from the vascular endothelium, platelets, neutrophils, and neurons.2 Upon oxidation to the quinonoid dihydrobiopterin (qBH2), BH4 is regenerated by dihydropteridine reductase (NAD[P]H:6,7-dihydropteridine oxidoreductase, EC 1.6.99.7;DHPR) using NADH as cofactor.3 BH4 and DHPR are ubiquitous.4 Their parallel distribution in some organs and blood cells which apparently do not synthesize catecholamine neurotransmitters and/or nitric oxide, implies that BH4 and DHPR may involve in other physiological functions.
      datePublished:1993
      isAccessibleForFree:
      hasPart:
         isAccessibleForFree:
         cssSelector:.main-content
         type:WebPageElement
      context:https://schema.org
Book:
      name:Chemistry and Biology of Pteridines and Folates
      isbn:
         978-1-4615-2960-6
         978-1-4613-6287-6
Organization:
      name:Springer US
      logo:
         url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
         type:ImageObject
      name:The University of Texas Medical Branch
      address:
         name:Department of Human Biological Chemistry and Genetics, The University of Texas Medical Branch, Galveston, USA
         type:PostalAddress
      name:The University of Texas Medical Branch
      address:
         name:Department of Human Biological Chemistry and Genetics, The University of Texas Medical Branch, Galveston, USA
         type:PostalAddress
ImageObject:
      url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
Person:
      name:Rong-sen Shen
      affiliation:
            name:The University of Texas Medical Branch
            address:
               name:Department of Human Biological Chemistry and Genetics, The University of Texas Medical Branch, Galveston, USA
               type:PostalAddress
            type:Organization
      name:Yixian Zhang
      affiliation:
            name:The University of Texas Medical Branch
            address:
               name:Department of Human Biological Chemistry and Genetics, The University of Texas Medical Branch, Galveston, USA
               type:PostalAddress
            type:Organization
PostalAddress:
      name:Department of Human Biological Chemistry and Genetics, The University of Texas Medical Branch, Galveston, USA
      name:Department of Human Biological Chemistry and Genetics, The University of Texas Medical Branch, Galveston, USA
WebPageElement:
      isAccessibleForFree:
      cssSelector:.main-content

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