NEWS OF THE WEEK SCIENTIFIC
PUBLISHING
STATUS REPORT ON OPEN ACCESS
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lishing released last week shows mixed results for the enterprise. Meanwhile, Wellcome Trust—the U.K.'s largest nongov ernmental funder of biomedical research—has now committed to open access. Sixty percent of surveyed openaccess journals are either making a profit or breaking even, says the study, which is billed as the first substantial effort of its kind. The study's sponsors are the Associa tion of Learned & Professional Society Publishers (ALPSP), the American Association for the Ad
Morris
WORK IN PROGRESS The structure of the active site alone says little about how nitrogenase works (iron, green; molybdenum, purple; sulfur, yellow; carbon, gray; oxygen, red; nitrogen, blue).
ENZYMOLOGY
NITROGENASE CAUGHT IN ACTION Intermediates in nitrogen fixation reaction are finally trapped
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as nitrogenases convert N 2 found in the environment into a form that can be used to make amino acids and other biologically valu able nitrogen compounds. A multidisciplinary team has now trapped N2-derived intermedi ates bound to a nitrogenase. This long-await ed achievement, the researchers say, may open the door to understanding how these enzymes work. "The structure ofnitrogenase and
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vancement of Science, and HighWire Press. The remaining 40% of open-access journals are not yet covering their costs and face an uncertain future, the study says. The report can be found at www. alpsp.org. The study revealed that most open-access journals do peer re view and some copyediting. They average five or six years old—an age when subscription journals are "well on the way to being finan cially stable," says ALPSP Chief Executive Sally Morris. One surprising finding is that author fees are less common than
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2005
its active site has been known for more than a decade," notes spectroscopist Brian M. Hoffman of Northwestern University. A complex metal cofactor in the multisubunit enzyme reduces N 2 to NH 3 . "But this structural in formation told us nothing about how this enzyme is able to bind and reduce substrates," Hoffman points out. For years, Hoffman has been working with biologist Dennis R. Dean of Virginia Tech and bio chemist Lance C. Seefeldt of Utah State University to figure out how to trap and characterize nitroge nase intermediates that might shed
in subscription journals. Open-ac cess journals rely more on grants, subsidies, and volunteer labor. Thus, "it doesn't follow that as the journals become more mature they would necessarily become more profitable," Morris says. Publisher Matthew Cockerill, of the open-access publishing firm BioMed Central, says the report "contains some useful information" but "draws many unwarranted conclusions. The fact that many open-access journals operate at a loss is simply a sign that these are early days." He adds that increased submissions and higher author fees are bringing BMC closer to profitability. Meanwhile, the Wellcome Trust has begun requiring grant recipients to deposit their research papers in the open-access PubMed Central article repository for re lease within six months of publi cation. Publishers are scrambling to develop a response.—SOPHIE ROVNER
light on the enzyme's mechanism. Now they've succeeded in trap ping the enzyme with N2-derived intermediates bound to the ac tive site (J. Am. Chem. Soc. 2005, 127,14960). "This is the break needed to get at the mechanism of this complex metalloenzyme," Seefeldt says. Guided by their previous ex periments with nonphysiological substrates, the researchers exposed subtly modified versions of the enzyme to N 2 or one of two sus pected dinitrogen intermediates and flash-froze the samples. Spec troscopy confirmed that they had indeed captured enzyme-bound intermediates. The team is now carrying out more spectroscopic work to de duce the structure of the trapped enzyme-bound intermediates. That work "should shed light on the most pressing questions about how nitrogenase works, including where N 2 binds to the active site and how it is reduced," Hoffman says.—AMANDA YARNELL WWW.CEN-0NLINE.ORG
