TECHNOLOGY
Johnson Wax Forges Ahead Into Its Second Century Privately owned since it was founded in 1886, S. C Johnson & Son Inc. ends year of centennial celebrations, looks to future stressing R&D Just before Christmas, ceremonies at Johnson Wax headquarters in Racine, Wis., marked the climax of a year of centennial activities. Since the company was founded in 1886, it has grown to become a major producer of specialty chemicals, with about 12,500 employees worldwide and with total annual sales of about $2 billion. Although everybody calls it Johnson Wax, the company's official name is S. C. Johnson & Son Inc. The first Samuel C. Johnson started out selling wood parquet floors. He also formulated and sold carnauba waxes, to use to polish the floors. The sideline grew to become the
main product and "Johnson Wax" became a household word. Research and development have always been important at Johnson, but especially in the past 35 years or so. The company's R&D staff has grown from three in 1920 to 70 in 1951, to more than 800 in 1986. Robert M. Fitch, senior vice president for R&D, notes that the R&D staff is particularly strong in such fields as colloid chemistry, rheology, and thin-film studies. Johnson's R&D effort, combined with astute marketing, certainly has been worthwhile in terms of successful products. Johnson brands hold significant market shares in such fields as home care products (Future, Pledge, Glade), insect control (Raid, Off), and personal care (Edge). In addition, the company markets a variety of products to commercial users. The company's forte originally was formulation. "We'd buy marketplace ingredients and mix them in unique ways," Fitch says. But
Johnson headquarters building was designed by Frank Lloyd Wright
Left, Johnson technician checks stain removal experiment; above, chairman Sam Johnson (left, foreground)greets runners in centennial relay race 16
January 5, 1987 C&EN
SCIENCE
Gene synthesis aids study of cytochrome
now, he says, "We're developing— and working to understand—our own raw materials." For instance, In an effort to better understand Johnson has developed a "unique" characteristics of the heme protein continuous process for making poly- cytochrome bs, including how amimers, notably low-molecular-weight no acid side chains determine the styrene-acrylic acid polymers. Among properties of the heme iron, rethe specialty chemicals that John- searchers have synthesized the gene son sells to other industrial users that encodes the protein and have are waterborne polymers (used for expressed it in bacteria. printing inks, adhesives, and coatA number of features make cytoings), oligomers for high-solids in- chrome b$ an ideal target for sitedustrial finishes, and rheology con- directed mutagenesis experiments, trol emulsions. says Stephen G. Sligar, biochemisOne thing Johnson doesn't make try professor at the University of or formulate anymore is waxes. The Illinois, Urbana. It plays an imporsolvent-type paste and liquid waxes tant role in electron transfer reacare now only a minor product line; tions, including reduction of cytothe company buys what it needs chrome P-450 in the liver and refrom contract suppliers. generation of ferrous hemoglobin Johnson has been a private com- in red blood cells. The protein's amipany since it was founded, with four no acid sequence is highly congenerations of Johnsons at its head. served among species, and a highHerbert F. Sr. succeeded father Sam- resolution crystal structure has been uel in 1919. Herbert F. Jr., who had determined for bovine cytochrome a 1922 chemistry degree from Cor- b5. nell, took over in 1928. His son, The problem, however, is that efalso Samuel C , became president forts to express native mammalian in 1966. cytochromes at high levels in a bacPerhaps partly as a result of being terial system have not been successa privately held firm, Johnson is ful. Why they have not been isn't unusual in several ways. For exam- entirely clear, Sligar says. ple, it's the only company with a To circumvent this problem and headquarters building designed by develop a method for producing naFrank Lloyd Wright. Wright buffs tive and mutant cytochrome b5 in still travel to Racine to admire the the large quantities needed for 46-year-old building, which is also biophysical characterization, Sligar, the subject of a recent book and of a postdoctoral fellow Susanne Beck current exhibit at the Milwaukee von Bodman, and Illinois professor art museum. of plant biology Mary A. Schuler Also, when Johnson's British sub- synthesized the gene in research sidiary had its 70th anniversary in supported by the National Institutes 1984, Sam Johnson flew the whole of Health [Proc. Natl Acad. Sci., 83, staff—more than 400 people—to 9443 (1986)]. This strategy gives the Racine at company expense for sev- researchers a number of advantages eral days' visit. And he plans to do over standard cloning techniques. the same thing for 280 Australian "The protein translation and synJohnson employees when that sub- thesis machinery of bacteria is very sidiary celebrates its 70th anniver- different from that of mammals," sary this coming June. Sligar points out. "Because we are The centennial celebration includ- building the gene from scratch, we ed a variety of events, ranging from can design the 5'-end of the gene to a company picnic (8000 attended) be utilized efficiently by the bacteto a series of R&D symposia, with rial system." Another advantage is talks by five Nobel Laureates in that synthesizing the gene allows Racine and one in the U.K. As the use of the redundancy of the genetcompany moves into its second cen- ic code both to match the codons to tury, it says it will continue to stress the bacterial transfer-RNA pool and R&D, because, as Sam Johnson puts to introduce restriction sites at conit, "Fresh ideas are the essence of venient places in the DNA for fuan assured future." ture mutagenesis efforts. Ward Worthy, Chicago The synthetic gene is expressed
efficiently in transformed Escherichia coli. For soluble cytochrome bs, about 8% of the total protein expressed by the bacteria is cytochrome fr5. Extensive characterization of this protein indicates that it is identical to soluble mammalian cytochrome b5. The complete cytochrome bs gene encodes a protein with an additional hydrophobic domain that interacts with cell membranes. The synthetic gene for the complete protein is expressed in E. coli, and the resultant protein is found in the plasma membrane. Efforts are under way to use the synthetic gene strategy to better understand the properties of cytochrome bs and its interaction with other proteins. It is naturally a sixcoordinate, low-spin heme protein with histidine residues at positions 39 and 63. These act as axial ligands to the heme iron. In one experiment, a mutant protein with methionine-63 was produced. Modeling studies had suggested that the sulfur of methionine would be too far removed from the heme iron to form an axial ligand, Sligar says. Characterization of the mutant cytochrome bs suggests that it is a stable, fivecoordinate, high-spin heme protein. The reduced mutant protein readily binds carbon monoxide with spectral characteristics similar to those observed for myoglobin and hemoglobin with bound carbon monoxide. The researchers also have produced mutant cytochrome b5 proteins with altered surface charges to investigate "docking" interactions between cytochrome b5 and its electron transfer partners. Heme-containing proteins have a wide range of properties, Sligar notes. Some activate oxygen, others bind and transport oxygen, still others transfer electrons. The differences presumably are due to differences in the protein environment around the heme and to differences in the axial ligands to the heme iron. Total gene synthesis, production, and characterization of such mutant heme proteins are being carried out by the Illinois researchers in an effort to establish a molecular basis for these differences, he says. Rudy Baum, San Francisco January 5, 1987 C&EN
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